Rapid Communication - Journal of Clinical and Bioanalytical Chemistry (2023) Volume 7, Issue 2
Improving peptide stability: Strategies and applications.
Notake Sezgin*Department of Chemistry, Yildiz Technical University, Istanbul, Turkey
- *Corresponding Author:
- Notake Sezgin
Department of Chemistry
Yildiz Technical University
Istanbul, Turkey
E-mail: notakesezgin@yildiz.edu.tr
Received: 29-Mar-2023, Manuscript No. AACBC-22-97775; Editor assigned: 30-Mar-2023, PreQC No. AACBC-22-97775(PQ); Reviewed: 14-Apr-2023, QC No. AACBC-22-97775; Revised: 19-Apr-2023, Manuscript No. AACBC-22-97775(R); Published: 25-Apr-2023, DOI:10.35841/aacbc-7.2.145
Citation: Sezgin N. Improving peptide stability: Strategies and applications. J Clin Bioanal Chem. 2023;7(2):145
Peptides are an essential class of biomolecules that play crucial roles in many physiological and biological processes. They are composed of amino acids, which are connected by peptide bonds to form short chains. Peptides are used in a wide range of applications, including as therapeutics, drug delivery agents, and food additives. However, one of the major challenges of using peptides is their inherent instability. In this article, we will discuss the factors that affect peptide stability and strategies to improve peptide stability [1].
Peptides are susceptible to various forms of degradation, which can result in loss of biological activity or even complete degradation of the peptide molecule. Some of the factors that affect peptide stability are: pH of peptide stability is highly dependent on pH. Peptides have an optimal pH range for stability, and outside this range, they can become unstable and degrade rapidly. Temperature of peptides are also sensitive to temperature changes. Elevated temperatures can lead to increased rates of peptide degradation, while low temperatures can cause conformational changes that can affect peptide stability [2].
Proteases proteases are enzymes that break down proteins and peptides. Peptides are susceptible to protease degradation, and this can occur both in vivo and in vitro. Oxidation peptides can also undergo oxidative degradation, which can lead to the formation of reactive oxygen species that can damage the peptide molecule. Aggregation: Peptides can also aggregate or clump together, which can cause them to become insoluble and lose their biological activity.
Given the challenges associated with peptide stability, it is essential to develop strategies to improve peptide stability. Here are some strategies that can be used to improve peptide stability: Chemical modifications can be used to improve peptide stability by altering the peptide's properties, such as charge, hydrophobicity, and conformational stability. For example, cyclization can increase peptide stability by reducing conformational flexibility and increasing resistance to protease degradation. Peptide analogs are peptides that have been modified to improve their stability and biological activity. These modifications can include the addition of nonnatural amino acids, modifications of peptide bonds, and incorporation of peptidomimetics [3].
Encapsulation: can be encapsulated in a protective matrix, such as a liposome or a polymer, to protect them from environmental factors such as temperature and proteases. Encapsulation can also improve peptide bioavailability and targeting. Stabilizing agents such as sugars, polyols, and surfactants can be used to improve peptide stability. These agents can prevent aggregation, oxidation, and protease degradation. The formulation of peptides can also be optimized to improve stability. This can include the addition of buffering agents to maintain pH, the use of stabilizing agents, and the optimization of storage conditions [4].
Stable peptides have a wide range of applications in various fields, including medicine, biotechnology, and food science. Here are some of the applications of stable peptides. Stable peptides are used as therapeutics for various diseases, including cancer, diabetes, and autoimmune disorders. These peptides can be designed to target specific receptors or enzymes, and their stability is critical for their efficacy. Drug delivery can also be used as drug delivery agents, allowing targeted delivery of drugs to specific cells or tissues. Encapsulation can protect peptides from degradation, allowing them to reach their intended targets intact [5].
References
- Sivaramaiah S, Raveendra Reddy P. Direct and derivative spectrophotometric determination of zinc with 2, 4-dihydroxybenzaldehyde isonicotinoyl hydrazone in potable water and pharmaceutical samples. J Anal Chem. 2005;60(9):828-32.
- Teixeira LS, Rocha FR, Korn M, et al. Flow-injection solid-phase spectrophotometry for the determination of zinc in pharmaceutical preparations. Anal Chim Acta. 1999;383(3):309-15.
- Matíes R, Jiménez F, Arias JJ, et al. Spectrofluorimetric determination of zinc with 1, 2, 4-trihydroxyanthraquinone in pharmaceutical preparations. Anal Lett. 1997;30(11):2059-70.
- Moody RR, Taylor RB. Determination of zinc in pharmaceutical preparations by atomic absorption spectrophotometry. J Pharm Pharmacol. 1972;24(11):848-52..
- Vani DS, Subudhi KS, Shivaramaiah S, et al. Direct and Derivative Spectrophotometric Determination of Zn (II) in Pharmaceuticals. Chem Sci Trans. 2013;2:513-23.
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