Akhlaghi M, Seyedalipour B, Pazhang M, Imani M (2025) The role of Gln269Leu mutation on the thermostability and structure of uricase from Aspergillus flavus. Sci Rep 15(1):8285. https://doi.org/10.1038/s41598-025-89605-w
Article CAS PubMed PubMed Central Google Scholar
Alves de Souza SM, de Araújo TS, Ferretti G, Kalume DE, Cordeiro Y, Almeida M, de Souza TLF (2022) Novel method for the production, purification, and characterization of recombinant Lunasin: identification of disulfide cross-linked dimers. Int J Pept Res Ther 28(6):159. https://doi.org/10.1007/s10989-022-10466-2
Arbouche N, Walch A, Raul J, Kintz P (2023) Intentional overdose of glargine insulin: determination of the parent compound in postmortem blood by < scp>LC-HRMS. J Forensic Sci 68(3):1077–1083. https://doi.org/10.1111/1556-4029.15247
Article CAS PubMed Google Scholar
Arkell K, Breil MP, Frederiksen SS, Nilsson B (2018) Mechanistic modeling of reversed-phase chromatography of insulins within the temperature range 10–40°C. ACS Omega 3(2):1946–1954. https://doi.org/10.1021/acsomega.7b01527
Article CAS PubMed PubMed Central Google Scholar
Ayan E, DeMirci H (2023) A brief atlas of insulin. Current Diabetes Reviews. https://doi.org/10.2174/1573399819666220610150342
Chavoshi F, Mirjalili SZ, Mohammadi A, Amini M, Somsen GW, Shirangi M (2024) Forced degradation products of Liraglutide: a comparative study of similarity between originator and analogue version by liquid chromatography–mass spectrometry. Int J Pept Res Ther 30(3):31. https://doi.org/10.1007/s10989-024-10608-8
Demelenne A, Napp A, Bouillenne F, Crommen J, Servais A-C, Fillet M (2019) Insulin aggregation assessment by capillary gel electrophoresis without sodium dodecyl sulfate: comparison with size-exclusion chromatography. Talanta 199:457–463. https://doi.org/10.1016/j.talanta.2019.02.074
Article CAS PubMed Google Scholar
Deschamps E, Calabrese V, Schmitz I, Hubert-Roux M, Castagnos D, Afonso C (2023) Advances in ultra-high-resolution mass spectrometry for pharmaceutical analysis. Molecules 28(5):2061. https://doi.org/10.3390/molecules28052061
Article CAS PubMed PubMed Central Google Scholar
Devi D, Sumithra M (2023) Development and validation of analytical technique for the evaluation of insulin glargine by RP-HPLC. Annals Phytomedicine Int J 12(1). https://doi.org/10.54085/ap.2023.12.1.73
Eeltink S, Ewonde RE, Papp D, Bui Q-D, Broeckhoven K, Scheich D, Lingg N, Pohl CA, Guillarme D (2025) The current state-of-the-art approaches and emerging opportunities for hydrophobic interaction chromatography for the characterization of intact proteins and biotherapeutics. J Chromatogr A 1756:466089. https://doi.org/10.1016/j.chroma.2025.466089
Article CAS PubMed Google Scholar
Evans AR, Mulholland J, Lewis MJ, Hu P (2024) Targeted CQA analytical control strategy for commercial antibody products: Replacing ion-exchange chromatography methods for charge heterogeneity with multi-attribute monitoring. MAbs. https://doi.org/10.1080/19420862.2024.2341641
Article PubMed PubMed Central Google Scholar
Fagan A, Bateman LM, O’Shea JP, Crean AM (2024) Elucidating the degradation pathways of human insulin in the solid state. J Anal Test 8(3):288–299. https://doi.org/10.1007/s41664-024-00302-5
Article CAS PubMed PubMed Central Google Scholar
Fingas F, Volke D, Hassert R, Fornefett J, Funk S, Baums CG, Hoffmann R (2019) Sensitive and immunogen-specific serological detection of Rodentibacter pneumotropicus infections in mice. BMC Microbiol 19(1):43. https://doi.org/10.1186/s12866-019-1417-7
Article PubMed PubMed Central Google Scholar
Gao J, Wang Y, Kraithong S, Jaisan C, Laosam P, Liang Y, Bunyameen N, Sangsawad P, Zhao Y (2026) Recent advances in the extraction, structural characterization, mechanisms and food applications of plant-derived peptides. Food Bioprocess Technol 19(2):66. https://doi.org/10.1007/s11947-025-04133-9
Goodarzi MM, Jalalirad R (2025) Clear insight into complex multimodal resins and impurities to overcome recombinant protein purification challenges: a review. Biotechnol Bioeng 122(1):5–29. https://doi.org/10.1002/bit.28846
Article CAS PubMed Google Scholar
Haduła J, Krepel ST, Babu D, Huang M, Boersma AJ (2025) Surface-modified protein crowders influence mutant huntingtin exon 1 aggregation via crowding effects, crowder association, and crowder solution stability. Protein Science. https://doi.org/10.1002/pro.70395
Article PubMed PubMed Central Google Scholar
Hazra P, Sreenivas S, Venkatesan K, Patale MB, Chatterjee A, Ramprabu N, Shaikh AM, Kusumanchi M (2021) A novel peptide design aids in the expression and its simplified process of manufacturing of Insulin Glargine in Pichia pastoris. Appl Microbiol Biotechnol 105(8):3061–3074. https://doi.org/10.1007/s00253-021-11224-y
Article CAS PubMed Google Scholar
Hwang HG, Kim KJ, Lee SH, Kim CK, Min CK, Yun JM, Son YJ (2016) Recombinant glargine insulin production process using Escherichia coli. J Microbiol Biotechnol 26(10):1781–1789
Article CAS PubMed Google Scholar
Jagschies G, Łącki KM (2018) Process Capability Requirements. In Biopharmaceutical Processing (pp. 73–94). Elsevier. https://doi.org/10.1016/B978-0-08-100623-8.00004-9
Jarosinski MA, Chen Y-S, Varas N, Dhayalan B, Chatterjee D, Weiss MA (2022) New horizons: next-generation insulin analogues: structural principles and clinical goals. J Clin Endocrinol Metab 107(4):909–928. https://doi.org/10.1210/clinem/dgab849
Article PubMed PubMed Central Google Scholar
Josic D, Kovac S (2010) Reversed-Phase High Performance Liquid Chromatography of Proteins. Curr Protocols Protein Sci 61(1). https://doi.org/10.1002/0471140864.ps0807s61
Kaki SB, Chintagunta AD, Prasad AN, Kumar NSS, Dirisala VR, Krishna MS, Naidu SJK, Ramesh B (2022a) Production and purification of recombinant glargine insulin from Escherichia coli BL-21 strain. Emergent Mater 5(2):335–346. https://doi.org/10.1007/s42247-021-00313-3
Kaki SB, Naga Prasad A, Chintagunta AD, Dirisala VR, Kumar S, Naidu NS, S. J. K., Ramesh B (2022b) Industrial scale production of recombinant human insulin using Escherichia coli BL-21. Iran J Sci Technol Trans A: Sci 46(2):373–383
Kasper CB (1970) Fragmentation of Proteins for Sequence Studies and Separation of Peptide Mixtures. In Protein Sequence Determination (pp. 137–184). Springer Berlin Heidelberg. https://doi.org/10.1007/978-3-662-12834-3_6
Khani S, Seyedjavadi SS, Hosseini HM, Goudarzi M, Barzegari M, Khatami S, Ajdary S, Eslamifar A, Amani J, Imani Fooladi AA, Razzaghi-Abyaneh M (2021) Recombinant expression of a plant-derived dimeric antifungal peptide (DiSkh-AMP1) joined by a flexible linker in Escherichia coli and evaluation of its biological activity in vitro. Int J Pept Res Ther 27(3):1967–1977. https://doi.org/10.1007/s10989-021-10225-9
Kiefer D, Bierscheid L, Kask O, Heyl C, Rehman S, Carmona J, Anderson KS, Fromme P (2025) Diverse approaches to isolate HLA class I molecules from bacterial inclusion bodies, forming heterotrimeric complexes. Protein Exp Purif 231:106713. https://doi.org/10.1016/j.pep.2025.106713
Kobl K, Nicoud L, Nicoud E, Watson A, Andrews J, Wilkinson EA, Shahid M, McKay C, Andrews BI, Omer BA, Narducci O, Masson E, Davies SH, Vandermeersch T (2024) Oligonucleotide purification by ion exchange chromatography: a step-by-step guide to process understanding, modeling, and simulation. Org Process Res Dev 28(7):2569–2589. https://doi.org/10.1021/acs.oprd.4c00013
Kovacevic N, Tariq AL-B, M (2022) Hydrophobic Interaction Chromatography: A Key Method for Protein Separation. J Nat Sci Eng 4(2). https://doi.org/10.14706/JONSAE2022421
Kuerzel GU, Shukla U, Scholtz HE, Pretorius SG, Wessels DH, Venter C, Potgieter MA, Lang AM, Koose T, Bernhardt E (2003) Biotransformation of insulin glargine after subcutaneous injection in healthy subjects. Curr Med Res Opin 19(1):34–40. https://doi.org/10.1185/030079902125001416
Article CAS PubMed Google Scholar
Kulkarni R, Bose K (2022) Protein Purification by Reversed Phase Chromatography and Hydrophobic Interaction Chromatography. In Textbook on Cloning, Expression and Purification of Recombinant Proteins (pp. 221–247). Springer Nature Singapore. https://doi.org/10.1007/978-981-16-4987-5_9
Kumar A, Tiwari S, Thavaselvam D, Sathyaseelan K, Prakash A, Barua A, Arora S, Kameswara Rao M (2012) Optimization and efficient purification of recombinant Omp28 protein of Brucella melitensis using Triton X-100 and β-mercaptoethanol. Protein Exp Purif 83(2):226–232. https://doi.org/10.1016/j.pep.2012.04.002
Li J-J, Liu Y-D, Wang F-W, Ma G-H, Su Z-G (2004) Hydrophobic interaction chromatography correctly refolding proteins assisted by glycerol and urea gradients. J Chromatogr A 1061(2):193–199. https://doi.org/10.1016/j.chroma.2004.11.002
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