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Pharmaceutics
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Protein Therapeutics in Biopharmaceutics
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Protein Therapeutics in Biopharmaceutics

A special issue of Pharmaceutics (ISSN 1999-4923). This special issue belongs to the section "Biopharmaceutics".

Deadline for manuscript submissions: closed (30 June 2022) | Viewed by 13204

Special Issue Editor

Dr. Joao Goncalves

E-Mail Website
Guest Editor
Research Institute for Medicines (iMed.ULisboa), Faculdade de Farmácia, Universidade de Lisboa, Avenida Professor Gama Pinto, 1649-003 Lisboa, Portugal
Interests: therapeutic antibody development
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protein drugs are the most active and fast-growing part in the field of drug research and development, and one of the most promising industries in the twenty-first century. Therapeutic protein drugs are an important class of medicines serving patients most in need of novel therapies. Protein drugs are developed to treat a wide variety of clinical indications, including cancers, autoimmune diseases, inflammation, diabetes neurodegenerative effects, exposure to infectious agents, and genetic disorders. Recent approved recombinant protein therapeutics has been used to target specific sites. A confluence of computational and high-throughput experimental methods for protein-engineering and “off the shelf” platform technologies has ushered in unprecedented opportunities to develop safe, effective, and more convenient protein therapeutics.

In this Special Issue, we invite authors to report their recently developed protein-based strategies for diagnosis and/or treatment of various disease states. We also welcome reviewer articles with expert opinions and perspectives in the protein therapeutics in biopharmaceutics field.

Dr. Joao Goncalves
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Pharmaceutics is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • therapeutics
  • protein Delivery
  • protein Production
  • theranostics
  • synthetic proteins
  • targeting
  • protein degradation
  • imaging
  • protein Engineering
  • gene Edition
  • gene Regulation
  • chimeric Proteins
  • protein conjugates

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Published Papers (4 papers)

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Research

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13 pages, 2322 KiB  
Article
Computation-Aided Design of Albumin Affibody-Inserted Antibody Fragment for the Prolonged Serum Half-Life
by Na Hyun Kwon, Jae Hun Lee and Inchan Kwon
Pharmaceutics 2022, 14(9), 1769; https://doi.org/10.3390/pharmaceutics14091769 - 24 Aug 2022
Cited by 2 | Viewed by 2623
Abstract
Single-chain variable fragments (scFvs) have been recognized as promising agents in cancer therapy. However, short serum half-life of scFvs often limits clinical application. Fusion to albumin affibody (ABD) is an effective and convenient half-life extension strategy. Although one terminus of scFv is available [...] Read more.
Single-chain variable fragments (scFvs) have been recognized as promising agents in cancer therapy. However, short serum half-life of scFvs often limits clinical application. Fusion to albumin affibody (ABD) is an effective and convenient half-life extension strategy. Although one terminus of scFv is available for fusion of ABD, it is also frequently used for fusion of useful moieties such as small functional proteins, cytokines, or antibodies. Herein, we investigated the internal linker region for ABD fusion instead of terminal region, which was rarely explored before. We constructed two internally ABD-inserted anti-HER2 4D5scFv (4D5-ABD) variants, which have short (4D5-S-ABD) and long (4D5-L-ABD) linker length respectively. The model structures of these 4D5scFv and 4D5-ABD variants predicted using the deep learning-based protein structure prediction program (AlphaFold2) revealed high similarity to either the original 4D5scFv or the ABD structure, implying that the functionality would be retained. Designed 4D5-ABD variants were expressed in the bacterial expression system and characterized. Both 4D5-ABD variants showed anti-HER2 binding affinity comparable with 4D5scFv. Binding affinity of both 4D5-ABD variants against albumin was also comparable. In a pharmacokinetic study in mice, the 4D5-ABD variants showed a significantly prolonged half-life of 34 h, 114 times longer than that of 4D5scFv. In conclusion, we have developed a versatile scFv platform with enhanced pharmacokinetic profiles with an aid of deep learning-based structure prediction. Full article
(This article belongs to the Special Issue Protein Therapeutics in Biopharmaceutics)
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18 pages, 1693 KiB  
Article
Analysis of Biologics Molecular Descriptors towards Predictive Modelling for Protein Drug Development Using Time-Gated Raman Spectroscopy
by Jaakko Itkonen, Leo Ghemtio, Daniela Pellegrino, Pia J. Jokela (née Heinonen), Henri Xhaard and Marco G. Casteleijn
Pharmaceutics 2022, 14(8), 1639; https://doi.org/10.3390/pharmaceutics14081639 - 5 Aug 2022
Cited by 2 | Viewed by 3013
Abstract
Pharmaceutical proteins, compared to small molecular weight drugs, are relatively fragile molecules, thus necessitating monitoring protein unfolding and aggregation during production and post-marketing. Currently, many analytical techniques take offline measurements, which cannot directly assess protein folding during production and unfolding during processing and [...] Read more.
Pharmaceutical proteins, compared to small molecular weight drugs, are relatively fragile molecules, thus necessitating monitoring protein unfolding and aggregation during production and post-marketing. Currently, many analytical techniques take offline measurements, which cannot directly assess protein folding during production and unfolding during processing and storage. In addition, several orthogonal techniques are needed during production and market surveillance. In this study, we introduce the use of time-gated Raman spectroscopy to identify molecular descriptors of protein unfolding. Raman spectroscopy can measure the unfolding of proteins in-line and in real-time without labels. Using K-means clustering and PCA analysis, we could correlate local unfolding events with traditional analytical methods. This is the first step toward predictive modeling of unfolding events of proteins during production and storage. Full article
(This article belongs to the Special Issue Protein Therapeutics in Biopharmaceutics)
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22 pages, 2481 KiB  
Article
Comprehensive Analysis of Nivolumab, A Therapeutic Anti-Pd-1 Monoclonal Antibody: Impact of Handling and Stress
by Anabel Torrente-López, Jesús Hermosilla, Antonio Salmerón-García, José Cabeza and Natalia Navas
Pharmaceutics 2022, 14(4), 692; https://doi.org/10.3390/pharmaceutics14040692 - 23 Mar 2022
Cited by 6 | Viewed by 3514
Abstract
Nivolumab, formulated in the medicine Opdivo® (10 mg/mL), is a therapeutic monoclonal antibody (mAb) used in the treatment of different types of cancer. Currently, there is insufficient knowledge about the behaviour of this protein with regards to the risk associated with its [...] Read more.
Nivolumab, formulated in the medicine Opdivo® (10 mg/mL), is a therapeutic monoclonal antibody (mAb) used in the treatment of different types of cancer. Currently, there is insufficient knowledge about the behaviour of this protein with regards to the risk associated with its routine handling or unintentional mishandling, or when subjected to stress conditions in hospitals. These conditions can be simulated in forced degradation studies, which provide an in-depth understanding of the biophysical and biochemical properties of mAbs. In this study, we carried out a physicochemical and functional characterisation of nivolumab, which was subjected to various stress conditions: heat, freeze/thaw cycles, agitation, light exposure and high hypertonic solution. We used a wide range of analytical techniques: Far-UV CD, IT-FS, DLS, SE/UHPLC(UV)-[Native]MS, and ELISA. The results show that exposure to light was the stress test with the greatest impact on the samples, revelling the formation of non-natural dimers and a different isoform profile. In addition, nivolumab (Opdivo®) demonstrated stability up to 60 °C (1 h). As regards functionality all the nivolumab (Opdivo®) stressed samples were found to be stable except for those subjected to light and agitation, and to a lesser extent, those subjected to FTC 5 and NaCl stresses. Full article
(This article belongs to the Special Issue Protein Therapeutics in Biopharmaceutics)
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Review

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23 pages, 2354 KiB  
Review
Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions
by Marina V. Pokrovskaya, Vadim S. Pokrovsky, Svetlana S. Aleksandrova, Nikolay N. Sokolov and Dmitry D. Zhdanov
Pharmaceutics 2022, 14(3), 599; https://doi.org/10.3390/pharmaceutics14030599 - 9 Mar 2022
Cited by 21 | Viewed by 3548
Abstract
L-asparaginases (EC 3.5.1.1) are a family of enzymes that catalyze the hydrolysis of L-asparagine to L-aspartic acid and ammonia. These proteins with different biochemical, physicochemical and pharmacological properties are found in many organisms, including bacteria, fungi, algae, plants and mammals. To date, asparaginases [...] Read more.
L-asparaginases (EC 3.5.1.1) are a family of enzymes that catalyze the hydrolysis of L-asparagine to L-aspartic acid and ammonia. These proteins with different biochemical, physicochemical and pharmacological properties are found in many organisms, including bacteria, fungi, algae, plants and mammals. To date, asparaginases from E. coli and Dickeya dadantii (formerly known as Erwinia chrysanthemi) are widely used in hematology for the treatment of lymphoblastic leukemias. However, their medical use is limited by side effects associated with the ability of these enzymes to hydrolyze L-glutamine, as well as the development of immune reactions. To solve these issues, gene-editing methods to introduce amino-acid substitutions of the enzyme are implemented. In this review, we focused on molecular analysis of the mechanism of enzyme action and to optimize the antitumor activity. Full article
(This article belongs to the Special Issue Protein Therapeutics in Biopharmaceutics)
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