Publications
38 results found
Almusaimi O, 2024, Peptide Therapeutics: Unveiling the Potential Against Cancer - A Journey Through 1989, Cancers, ISSN: 2072-6694
Almusaimi O, 2024, Exploring FDA-Approved Frontiers: Insights into Natural and Engineered Peptide Analogues in GLP-1, GIP, GHRH, CCK, ACTH, and α-MSH Realms, Biomolecules, ISSN: 2218-273X
Zulfiqar N, Nadeem R, Almusaimi O, 2024, Photocatalytic degradation of antibiotics via exploitation of magnetic nanocomposite: a green nanotechnology approach towards drug-contaminated wastewater reclamation, ACS Omega, Vol: 9, Pages: 7986-8004, ISSN: 2470-1343
In the quest for eco-conscious innovations, this research was designed for the sustainable synthesis of magnetite (Fe3O4) nanoparticles, using ferric chloride hexahydrate salt as a precursor and extract of Eucalyptus globulus leaves as both a reducing and capping agent, which are innovatively applied as a photocatalyst for the photocatalytic degradation of antibiotics “ciprofloxacin and amoxicillin”. Sugar cane bagasse biomass, sugar cane bagasse pyrolyzed biochar, and magnetite/sugar cane bagasse biochar nanocomposite were also synthesized via environmentally friendly organized approaches. The optimum conditions for the degradation of ciprofloxacin and amoxicillin were found to be pH 6 for ciprofloxacin and 5 for amoxicillin, dosage of the photocatalyst (0.12 g), concentration (100 mg/L), and irradiation time (240 min). The maximum efficiencies of percentage degradation for ciprofloxacin and amoxicillin were found to be (73.51%) > (63.73%) > (54.57%) and (74.07%) > (61.55%) > (50.66%) for magnetic nanocomposites, biochar, and magnetic nanoparticles, respectively. All catalysts demonstrated favorable performance; however, the “magnetite/SCB biochar” nanocomposite exhibited the most promising results among the various catalysts employed in the photocatalytic degradation of antibiotics. Kinetic studies for the degradation of antibiotics were also performed, and notably, the pseudo-first-order chemical reaction showed the best results for the degradation of antibiotics. Through a comprehensive and comparative analysis of three unique photocatalysts, this research identified optimal conditions for efficient treatment of drug-contaminated wastewater, thus amplifying the practical significance of the findings. The recycling of magnetic nanoparticles through magnetic separation, coupled with their functional modification for integration into composite materials, holds significant application potential in the degradation of antibiotics.
Al Shaer D, Al Musaimi O, Albericio F, et al., 2024, 2023 FDA TIDES (Peptides and Oligonucleotides) Harvest., Pharmaceuticals (Basel), Vol: 17, ISSN: 1424-8247
A total of nine TIDES (pepTIDES and oligonucleoTIDES) were approved by the FDA during 2023. The four approved oligonucleotides are indicated for various types of disorders, including amyotrophic lateral sclerosis, geographic atrophy, primary hyperoxaluria type 1, and polyneuropathy of hereditary transthyretin-mediated amyloidosis. All oligonucleotides show chemically modified structures to enhance their stability and therapeutic effectiveness as antisense or aptamer oligomers. Some of them demonstrate various types of conjugation to driving ligands. The approved peptides comprise various structures, including linear, cyclic, and lipopeptides, and have diverse applications. Interestingly, the FDA has granted its first orphan drug designation for a peptide-based drug as a highly selective chemokine antagonist. Furthermore, Rett syndrome has found its first-ever core symptoms treatment, which is also peptide-based. Here, we analyze the TIDES approved in 2023 on the basis of their chemical structure, medical target, mode of action, administration route, and common adverse effects.
Varshitha G, Othman A, Colin B, et al., 2023, Determining the hydrophobicity index of protected amino acids and common protecting groups, Separations, Vol: 10, Pages: 1-11, ISSN: 2297-8739
Peptides are in great demand in the pharmaceutical arena and a majority of these peptides contain 20 or more amino acids. They are infrequently synthesised using the fragment condensation approach. A key limitation in adopting this approach more commonly is that protected peptide fragments with high purity are often required prior to the final condensation steps. It is hypothesized that understanding the hydrophobic nature of the protected amino acids will assist with designing optimal fragment purification processes when needed. Whilst a myriad of hydrophobicity indices are reported in the literature for unprotected amino acids, the literature lacks any data regarding the protected amino acids which form the key precursor for the fragment condensation task. In this current study, hydrophobicity indices for protected amino acids with common α-amino and sidechain protecting groups were experimentally determined. Different positions for each amino acid within the peptide chain were considered, namely at the C-terminal and N-terminal as well as internal positions. These data give deep insights on the hydrophobicity of each amino acid with respect to its position in the peptide chain. The data acquired in this research facilitated the prediction of the retention time of protected peptide fragments with an uncertainty of less than ±1.5%.
Almusaimi O, Williams D, 2023, Methods of Chemical Synthesis of Peptides - GB2309538.3, Patent
Almusaimi O, Al Shaer D, Albericio F, et al., 2023, 2022 FDA TIDES (peptides and oligonucleotides) harvest, Pharmaceuticals, Vol: 16, ISSN: 1424-8247
A total of 37 new drug entities were approved in 2022; although that year registered the lowest number of drug approvals since 2016, the TIDES class consolidated its presence with a total of five authorizations (four peptides and one oligonucleotide). Interestingly, 23 out of 37 drugs were first-in-class and thus received fast-track designation by the FDA in categories such as breakthrough therapy, priority review voucher, orphan drug, accelerated approval, and so on. Here, we analyze the TIDES approved in 2022 on the basis of their chemical structure, medical target, mode of action, administration route, and common adverse effects.
Al Musaimi O, Morse SV, Lombardi L, et al., 2023, Successful synthesis of a glial-specific blood-brain barrier shuttle peptide following a fragment condensation approach on a solid-phase resin, Journal of Peptide Science, Vol: 29, Pages: 1-9, ISSN: 1075-2617
Successful manual synthesis of the TD2.2 peptide acting as a blood-brain barrier shuttle was achieved. TD2.2 was successfully synthesised by sequential condensation of four protected peptide fragments on solid-phase settings, after several unsuccessful attempts using the stepwise approach. These fragments were chosen to minimize the number of demanding amino acids (in terms of coupling, Fmoc removal) in each fragment that are expected to hamper the overall synthetic process. Thus, the hydrophobic amino acids as well as Fmoc-Arg (Pbf)-OH were strategically spread over multiple fragments rather than having them congested in one fragment. This study shows how a peptide that shows big challenges in the synthesis using the common stepwise elongation methodology can be synthesised with an acceptable purity. It also emphasises that choosing the right fragment with certain amino acid constituents is key for a successful synthesis. It is worth highlighting that lower amounts of reagents were required to synthesise the final peptide with an identical purity to that obtained by the automatic synthesiser.
Almusaimi O, Mercado-Valenzo OM, Williams DR, 2023, Factors influencing the prediction accuracy of model peptides in reversed-phase liquid chromatography, Separations, Vol: 10, Pages: 1-37, ISSN: 2297-8739
Hydrophobicity is an important physicochemical property of peptides in solution. As well as being strongly associated with peptide stability and aggregation, hydrophobicity governs the solution based chromatographic separation processes, specifically reversed-phase liquid chromatography (RPLC). In addition, hydrophobicity is a major physicochemical property of peptides in comparison to H-bonding, electrostatic, and aromatic properties in intermolecular interactions. However, a wide range of molecular factors can influence peptide hydrophobicity, with accurate predictions depending on specific peptide amino acid compositions, structure, and conformation. It is noticeable that peptide composition, the position of the amino acid, and its neighbouring groups play a crucial role in the elution process. In light of this, the same amino acid behaved differently depending on its position and neighbouring amino acid in the peptide chain. Extra attention should be paid to the denaturation process during the course of elution, as it has been shown to complicate and alter the elution pattern. This paper reports on the key peptide properties that can alter hydrophobicity and, consequently, the RPLC elution behaviour of the peptides, and it will conclude by proposing improved prediction algorithms for peptide elution in RPLC.
Al Musaimi O, Gavva V, Williams DR, 2023, Greener cleavage of protected peptide fragments from Sieber Amide Resin., ChemistryOpen, Vol: 11, Pages: 1-7, ISSN: 2191-1363
Following the successful introduction of two benign solvents for cleaving protected acid peptide fragments from 2-chlorotrityl chloride (2-CTC) resin, there is a need to green the cleavage process for obtaining protected peptide amide fragments. In this work, p-xylene and toluene are introduced as greener alternates to dichloromethane (DCM) for preparing protected peptide amide fragments from a Sieber amide resin. The N-dealkylation is a demanding chemical reaction, requiring that the cleavage protocol be optimised to ensure complete cleavage from the resin. After a 30 min reaction time, only 66 % of the final peptide product was retrieved even with the conventional dichloromethane solvent. Therefore, 120 min was considered sufficient to fully cleave the peptide from the Sieber amide resin. This work reaffirms the fact that greening strategies are far from detrimental, with green alternatives often outperforming their replaced counterparts.
Al Musaimi O, Valenzo OMM, Williams DR, 2023, Prediction of peptides retention behavior in reversed-phase liquid chromatography based on their hydrophobicity, Journal of Separation Science, Vol: 46, Pages: 1-17, ISSN: 1615-9306
Hydrophobicity is an important physicochemical property of peptides and proteins. It is responsible for their conformational changes, stability, as well as various chemical intramolecular and intermolecular interactions. Enormous efforts have been invested to study the extent of hydrophobicity and how it could influence various biological processes, in addition to its crucial role in the separation and purification endeavor as well.Here, we have reviewed various studies that were carried out to determine the hydrophobicity starting from (i) simple amino acids solubility behavior, (ii) experimental approach that was undertaken in the reversed-phase liquid chromatography mode, and ending with (iii) some examples of more advanced computational and machine learning models.
Zulfiqar N, 2023, Photocatalytic Degradation of Antibiotics From Aqueous Solution via Exploitation of Magnetic Nanocomposite: a Green Nanotechnology Approach Towards Drug-infested Water Reclamation, SSRN Electronic Journal
Almusaimi O, Lombardi L, Williams D, et al., 2022, Strategies for improving peptide stability and delivery, Pharmaceuticals, Vol: 15, ISSN: 1424-8247
Peptides play an important role in many fields, including immunology, medical diagnostics, and drug discovery, due to their high specificity and positive safety profile. However, for their delivery as active pharmaceutical ingredients, delivery vectors, or diagnostic imaging molecules, they suffer from two serious shortcomings: their poor metabolic stability and short half-life. Major research efforts are being invested to tackle those drawbacks, where structural modifications and novel delivery tactics have been developed to boost their ability to reach their targets as fully functional species. The benefit of selected technologies for enhancing the resistance of peptides against enzymatic degradation pathways and maximizing their therapeutic impact are also reviewed. Special note of cell-penetrating peptides as delivery vectors, as well as stapled modified peptides, which have demonstrated superior stability from their parent peptides, are reported.
Albericio F, Jaradat DMM, Al Musaimi O, 2022, Advances in solid-phase peptide synthesis in aqueous media (ASPPS), Green Chemistry, Vol: 24, ISSN: 1463-9262
Peptides are gaining ground in the pharmaceutical arena, with a total of 22 approvals over the last six years. These molecules are also present in antibody-drug conjugate constructs as linkers or payloads, or both. Solid-phase peptide synthesis (SPPS) is the method of choice for peptide synthesis. The introduction of the automatic synthesizer has facilitated this methodology and helped reduce the amounts of solvents needed. However, there are still concerns regarding the amounts, as well as the safety profiles, of the solvents involved in SPPS. Here we discuss work addressing the use of water as the greenest alternative to the common non-green solvents employed in various steps of the SPPS methodology. Various technologies were introduced which enabled the synthesis in aqueous media of di- and up to decapeptide with satisfactory yields and purities
Al Shaer D, Almusaimi O, Albericio F, et al., 2022, 2021 FDA TIDES (peptides and oligonucleotides) harvest, Pharmaceuticals, Vol: 15, ISSN: 1424-8247
From the medical, pharmaceutical, and social perspectives, 2021 has been a year dominated by the COVID-19 pandemic. However, despite this global health crisis, the pharmaceutical industry has continued its endeavors, and 2021 could be considered an excellent year in terms of the drugs accepted by the US Food and Drug Administration (FDA). Thus, during this year, the FDA has approved 50 novel drugs, of which 36 are new chemical entities and 14 biologics. It has also authorized 10 TIDES (8 peptides, 2 oligonucleotides), in addition to 2 antibody-drug conjugates (ADCs) whose structures contain peptides. Thus, TIDES have accounted for about 24% of the approvals in the various drug categories. Importantly, this percentage has surpassed the figure in 2020 (10%), thus reflecting the remarkable success of TIDES. In this review, the approved TIDE-based drugs are analyzed on the basis of their chemical structure, medical target, mode of action, administration route, and adverse effects.
Almusaimi O, Albericio F, de la Torre B, 2021, Propylphosphonic anhydride (T3P) as green coupling reagent for solid-phase peptide synthesis, Bonding Through Chemistry, ACS spring 2022
Al Musaimi O, Wisdom R, Talbiersky P, et al., 2021, Propylphosphonic anhydride (T3P®) as coupling reagent for solid‐phase peptide synthesis, ChemistrySelect, Vol: 6, Pages: 2649-2657, ISSN: 2365-6549
Amidation is the predominant reaction within the pharmaceutical setting, and it is attracting greater attention due to the increased demand for therapeutic peptides. The high therapeutic efficacy and safety profile of peptides have placed these molecules in prime position within the pharmaceutical arena, which is reflected by these molecules receiving several approvals from various regulatory agencies each year. In this context, the demand for developing efficient strategies for peptide synthesis has also risen. Although propylphosphonic anhydride (T3P®), which has been recently proposed as a green coupling reagent, has shown good performance in solution, it has never been applied to solid‐phase peptide synthesis (SPPS). Here we test the use of T3P® for SPPS. Satisfactory yields were achieved with a mild activation protocol. Various green solvents were tested and proved to be compatible with this coupling reagent. Several commonly used reagents cause allergic reactions or are susceptible to explosion under certain conditions. To overcome these issues, we propose T3P® as a potential alternative coupling reagent in SPPS.
Al Musaimi O, Al Shaer D, Albericio F, et al., 2021, 2020 FDA TIDES (peptides and oligonucleotides) harvest, Pharmaceuticals, Vol: 14, ISSN: 1424-8247
2020 has been an extremely difficult and challenging year as a result of the coronavirus disease 2019 (COVID-19) pandemic and one in which most efforts have been channeled into tackling the global health crisis. The US Food and Drug Administration (FDA) has approved 53 new drug entities, six of which fall in the peptides and oligonucleotides (TIDES) category. The number of authorizations for these kinds of drugs has been similar to that of previous years, thereby reflecting the consolidation of the TIDES market. Here, the TIDES approved in 2020 are analyzed in terms of chemical structure, medical target, mode of action, and adverse effects.
Al Shaer D, Almusaimi O, de la Torre BG, et al., 2020, Hydroxamate siderophores: natural occurrence, chemical synthesis, iron binding affinity and use as Trojan horses against pathogens., European Journal of Medicinal Chemistry, Vol: 208, Pages: 1-31, ISSN: 0223-5234
Hydroxamic acids are an important class of molecules, in particular because of their metal-chelating ability. Microorganisms, including pathogenic bacteria, use hydroxamate-based entities (siderophores), among others, to acquire Fe (III). The "Trojan horse" strategy exploits the need of bacteria for this metal by using Fe (III) active transporters to carry antibacterial or bactericidal moieties into the bacterial cell. Many natural Trojan horses (sideromycins) are derived from hydroxamic acids, thereby reflecting their potency. Various artificial sideromycins and their antibacterial activities have been reported. This review discusses the structural aspects of the hydroxamate-siderophores isolated in the last two decades, the chemical synthesis of their building blocks, their binding affinity towards Fe (III), and their application as Trojan horses (weaknesses and strengths).
Al Musaimi O, SUMMERS BD, Alhassan M, et al., 2020, Analytical methodologies to assure successful peptide synthesis when utilizing polystyrene/DVB resins, Chimica Oggi/Chemistry Today, Vol: 38, Pages: 48-51, ISSN: 0392-839X
Solid-phase peptide synthesis has become an important technique as the method of choice to deliver high quality peptide entities at both laboratory and production scale. The polymeric support (i.e. the resin) is the most essential part of the process as it covalently holds the growing peptide through the various synthetic steps. Several key features of the resin must be addressed before initiation of the synthesis to ensure successful generation of the desired peptide. In this paper, several PuroSynthTM peptide synthesis resins were examined for a range of aspects including morphological characteristics, mechanical stability and distribution of functional groups. Additionally, to demonstrate the effect of these aspects, the Purosynth™ CTC resin was used to synthesise a heptapeptide analogue to the antibiotic darobactin with >95 % purity.
Alhassan M, Al Musaimi O, Collins JM, et al., 2020, Cleaving protected peptides from 2-chlorotrityl chloride resin. Moving away from dichloromethane, Green Chemistry, Vol: 22, Pages: 2840-2845, ISSN: 1463-9262
In recent years, the work of various research groups has allowed the substitution of the hazardous solvents most widely used in solid-phase peptide synthesis, namely DMF, NMP, DCM, DEE, among others, by several much less hazardous solvents. Indeed, greener alternatives have been found for almost all steps of the process, with the exception of the cleavage of protected peptides from 2-chlorotrityl chloride resin. Here, after careful screening of several of the so-called green solvents, we propose 2% TFA in either anisole or 1,3-dimethoxybenzene as optimal for the cleavage step. The higher boiling point of these solvents compared with the DCM allows the preparation of protected peptides with less risk of premature removal of the most labile protecting groups, such as the Trt of His. Our findings once again evidence the value/versatility of green solvents in strict chemical terms.
Musaimi OAL, Summers BD, Basso A, et al., 2020, Combining solid phase synthesis and chromatographic purification for efficient peptide manufacture, Chimica Oggi/Chemistry Today, Vol: 38, Pages: 18-21, ISSN: 0392-839X
In recent years, peptides have gained an important position in the drug arena for a variety of treatments. Solid-phase peptide synthesis (SPPS) continues to have a significant impact in both R&D as well as in production of commercial peptides. The combination of SPPS with reverse-phase (RP) chromatographic separations allowed for the peptides to be purified to levels suitable for drug usage. Thanks to their chemical and physical stability to high pressure, chemicals, temperature and oxidising reagents, polystyrene / divinyl benzene (PS/DVB) resins are the main solid support for peptide synthesis as well as being suitable for the chromatographic purification of the peptides by RP and ion exchange (IEX). Depending on the application, the optimal cross-linking changes, as do the optimal particle size, the uniformity in particle size distribution and the porosity of the resin. The characteristics and applications of the PS/DVB resins are explored in this paper for the synthesis and purification of peptides of commercial interest.
Al Shaer D, Al Musaimi O, Albericio F, et al., 2020, 2019 FDA TIDES (Peptides and Oligonucleotides) Harvest, Pharmaceuticals, Vol: 13, Pages: 1-15, ISSN: 1424-8247
2019 has been an excellent year in terms of peptides and oligonucleotides (TIDES) approved by the FDA. Despite the drop in the number of total drugs approved by the FDA in 2019 in comparison with 2018 (48 vs. 59), the total number of TIDES authorized increased (seven vs. three). Year after year, TIDES are increasingly present in therapy, as imaging agents, theragnostic and constituent moieties of other complex drugs, such as antibody drug conjugates. This means a consolidation of these kinds of drugs in the pharmaceutical arena, paving the way in the coming years for the approval of others for diverse medical indications. Here the TIDES approved in 2019 are analyzed in terms of chemical structure, medical target, mode of action, and adverse effects.
Al Musaimi O, de la Torre BG, Albericio F, 2020, Greening Fmoc/tBu solid-phase peptide synthesis, Green Chemistry, Vol: 22, Pages: 996-1018, ISSN: 1463-9262
Peptides are gaining considerable attention as potential drugs. The so-called Fmoc/tBu solid-phase synthesis is the method of choice for the synthesis of these molecules in both research and industrial settings. This synthetic strategy involves a solid polymeric protecting group and allows the use of an excess of reagents to achieve quantitative yields. Intermediates are not isolated. However, extensive washing with solvents is carried out between the synthetic steps. Hazardous solvents, mainly DMF, NMP, and CH2Cl2, are currently being used for the chemical reactions and also for the washings. In recent years, several studies have proposed the use of greener solvents in solid-phase peptide synthesis (SPPS). Here we compile all the greening efforts done in this regard and analyze each synthetic step separately. In summary, we can conclude that in many cases green solvents do not impair the synthetic process and that their adoption in current synthetic schemes will be translated into a smaller impact on the environment and on human health.
Almusaimi O, Basso A, de la Torre BG, et al., 2019, Calculating resin functionalization in solid-phase peptide synthesis using a standardized method based on Fmoc determination, ACS combinatorial science, Vol: 21, Pages: 717-721, ISSN: 2156-8944
Solid-phase synthesis is the method of choice for peptide preparation in both research and industrial settings. The whole synthetic process is governed by the initial functionalization of the resin. Although the literature provides several methods to determine such functionalization, the addition of an Fmoc-amino acid and the posterior spectrophotometric measurement of the dibenzofulvene adduct formed after Fmoc removal is the most widely used for this purpose. However, a range of molar extinction coefficient (ε) values and even wavelengths are currently used in the field, with no standardization of the method. Here, we propose a single-point standardization method that involves a standard solution of the corresponding amino acid to be checked that is prepared freshly at the time of the analysis.
Al Musaimi O, El-Faham A, Basso A, et al., 2019, γ-Valerolactone (GVL): An eco-friendly anchoring solvent for solid-phase peptide synthesis, Tetrahedron Letters, Vol: 60, Pages: 151058-151058, ISSN: 0040-4039
Due to the hazardous nature of CH2Cl2, regulatory authorities have imposed restrictions to minimize or even stop its use. It has therefore become imperative to identify environmentally benign solvents to replace it. Here we report on a bio derived solvent, γ-valerolactone, for the incorporation of the first amino acid onto p-alkoxybenzyl alcohol resin in solid-phase peptide synthesis. Satisfactory loading values (by a spectrophotometric method) were achieved. Furthermore, racemization and dipeptide formation were also checked and found to be acceptable.
Al Musaimi O, El-Faham A, Almarhoon Z, et al., 2019, Bypassing osmotic shock dilemma in a polystyrene resin using the green solvent cyclopentyl methyl Ether (CPME): a morphological perspective, Polymers, Vol: 11, Pages: 1-13, ISSN: 2073-4360
The “osmotic shock” phenomenon is the main thing that is responsible for morphological structure alteration, which can jeopardize the use of a polymer in a chemical process. This is extremely important in solid-phase peptide synthesis (SPPS), which is the method of choice for the preparation of these important biologically active compounds. Herein, we have used Hildebrand solubility parameters (δ) to investigate the influence of different ethers that are used in the precipitation step of the SPPS using a polystyrene resin. The green cyclopentyl methyl ether (CPME) has shown to be slightly superior to 2-methyltetrahydrofurane, which is also a green ether and clearly better than the hazardous diethyl ether and tert-butyl methyl ether. These results have been corroborated by scanning electron microscope (SEM) analysis and computational studies. All together, these confirm the adequacy of CPME for being the ether of choice to be used in SPPS.
Al Shaer D, Al Musaimi O, Albericio F, et al., 2019, 2018 FDA tides harvest, Pharmaceuticals, Vol: 12, Pages: 1-6, ISSN: 1424-8247
In 2018, the United States Food and Drug Administration (FDA) approved a total of 59 new drugs, three of them (5%) are TIDES (or also, -tides), two oligonucleotides and one peptide. Herein, the three TIDES approved are analyzed in terms of medical target, mode of action, chemical structure, and economics.
Musaimi OAL, Serban S, Jad YE, et al., 2019, New manufacturing process to produce highly uniform resins with excellent performances in Solid Phase Peptide Synthesis, Chimica Oggi/Chemistry Today, Vol: 37, Pages: 8-10, ISSN: 0392-839X
Peptides are an important class of Active Pharmaceutical Ingredients. Thanks to the implementation of the solid phase synthesis methodology pioneered by the Nobel Laureate R. Bruce Merrifield in the 20th century, it is now possible to synthesize peptides with up to forty amino acids in a multi- kilogram scale. Herein, we describe a new manufacturing process to produce highly uniform resins that can be successfully applied to solid phase peptide synthesis (SPPS). The resins were employed for the synthesis of between 5 and 28mer peptides using either automatic heat-assisted microwave systems or manual mode. Excellent results are reported when PuroSynth™ CTC/S, PuroSynth™ Wang/S, PuroSynth™ Rink Amide/S and PuroSynth™ MBHA/S are used for SPPS.
Musaimi OAL, Serban S, Jad YE, et al., 2019, Jetting manufacturing of resins for solid-phase peptide synthesis, Chimica Oggi/Chemistry Today, Vol: 37, Pages: 20-23, ISSN: 0392-839X
Peptides are an important class of Active Pharmaceutical Ingredients. Indeed, it is now feasible to synthesize peptides of up to forty amino acids in a multi-kilogram scale. This achievement has been made thanks to the implementation of the solid-phase synthesis methodology described by the Nobel Laureate R. Bruce Merrifield in 1963. Successful solid-phase peptide synthesis depends directly on the quality of the polymeric support, namely the resin. Here we describe new polystyrene in-house resins produced by 'Jetting' technology. The excellent properties (swelling, loading, particle size distribution, morphological structure) of these resins assure the quality of the final peptide.
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