Abstract
Since proteins and peptides play critical roles in many biological phenomena, their use as drugs is of great interest. However, their development is limited due to their poor bioavailability, antigenicity and unfavorable pharmacokinetics. In the majority of cases, not all domains of proteins are essential protein-protein interactions necessary for biological activities but only small regions of their folded structure, perform the interactions. Usually, these particular secondary structures are β-turns, occurring on the exposed surface of proteins, constitute the functional elements involved in molecular recognition processes between proteins, and in interactions between ligands and receptors. Moreover, there are also several examples of the design of modified peptides as therapeutic agents by mimicking β-turn structures. In view of this, this review will be focused on the importance of β-turn in some biological phenomena, such as prohormone proteolytic processing. This report will also address the use of β-turn mimicking strategies and its application in the design of potent peptide analogues which play an equally important role. Due to the optimal surface conformation, β-turn mimetics lead to productive interaction with receptors and antibodies.
Keywords: β-Turn, secondary structure, receptor, analog, posttranslational modification, prohormone convertases, precursor, substrate dynamics
Central Nervous System Agents in Medicinal Chemistry
Title: Functional Role of β-Turn in Polypeptide Structure and its use as Template to Design Therapeutic Agents
Volume: 6 Issue: 3
Author(s): Noureddine Brakch, Boutaina El Abida and Mohamed Rholam
Affiliation:
Keywords: β-Turn, secondary structure, receptor, analog, posttranslational modification, prohormone convertases, precursor, substrate dynamics
Abstract: Since proteins and peptides play critical roles in many biological phenomena, their use as drugs is of great interest. However, their development is limited due to their poor bioavailability, antigenicity and unfavorable pharmacokinetics. In the majority of cases, not all domains of proteins are essential protein-protein interactions necessary for biological activities but only small regions of their folded structure, perform the interactions. Usually, these particular secondary structures are β-turns, occurring on the exposed surface of proteins, constitute the functional elements involved in molecular recognition processes between proteins, and in interactions between ligands and receptors. Moreover, there are also several examples of the design of modified peptides as therapeutic agents by mimicking β-turn structures. In view of this, this review will be focused on the importance of β-turn in some biological phenomena, such as prohormone proteolytic processing. This report will also address the use of β-turn mimicking strategies and its application in the design of potent peptide analogues which play an equally important role. Due to the optimal surface conformation, β-turn mimetics lead to productive interaction with receptors and antibodies.
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Cite this article as:
Brakch Noureddine, El Abida Boutaina and Rholam Mohamed, Functional Role of β-Turn in Polypeptide Structure and its use as Template to Design Therapeutic Agents, Central Nervous System Agents in Medicinal Chemistry 2006; 6 (3) . https://dx.doi.org/10.2174/187152406778226707
DOI https://dx.doi.org/10.2174/187152406778226707 |
Print ISSN 1871-5249 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6166 |
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