caa a22 4500 463186559 CHVBK 20180406164855.0 cr unu---uuuuu 170326e20071101xx s 000 0 eng 10.1007/s00726-006-0458-z doi (NATIONALLICENCE)springer-10.1007/s00726-006-0458-z Peptidology: short amino acid modules in cell biology and immunology [Elektronische Daten] [G. Lucchese, A. Stufano, B. Trost, A. Kusalik, D. Kanduc] Summary.: Short amino acid motifs, either linear sequences or discontinuous amino acid groupings, can interact with specific protein domains, so exerting a central role in cell adhesion, signal transduction, hormone activity, regulation of transcript expression, enzyme activity, and antigen-antibody interaction. Here, we analyze the literature for such critical short amino acid motifs to determine the minimal peptide length involved in biologically important interactions. We report the pentapeptide unit as a common minimal amino acid sequence critically involved in peptide-protein interaction and immune recognition. The present survey may have implications in defining the dimensional module for peptide-based therapeutical approaches such as the development of novel antibiotics, enzyme inhibitors/activators, mimetic agonists/antagonists of neuropeptides, thrombolitic agents, specific anti-viral agents, etc. In such a therapeutical context, it is of considerable interest that low molecular weight peptides can easily cross biological barriers, are less susceptible to protease attacks, and can be administered at high concentrations. In addition, small peptides are a rational target for strategies aimed at antigen-specific immunotherapeutical intervention. As an example, specific short peptide fragments might be used to elicit antibodies capable of reacting with the full-length proteins containing the peptide fragment's amino acid sequence, so abolishing the risk of cross-reactivity. Springer-Verlag, 2006 Keywords: Regulatory peptides - Epitopic peptides - Minimal peptide length - Pentapeptide unit nationallicence Lucchese G. Department of Biochemistry and Molecular Biology "Ernesto Quagliariello”, University of Bari, Bari, Italy aut Stufano A. Department of Biochemistry and Molecular Biology "Ernesto Quagliariello”, University of Bari, Bari, Italy aut Trost B. Department of Computer Science, University of Saskatchewan, Saskatoon, Canada aut Kusalik A. Department of Computer Science, University of Saskatchewan, Saskatoon, Canada aut Kanduc D. Department of Biochemistry and Molecular Biology "Ernesto Quagliariello”, University of Bari, Bari, Italy aut Amino Acids Springer-Verlag 33/4(2007-11-01), 703-707 0939-4451 33:4<703 2007 33 726 https://doi.org/10.1007/s00726-006-0458-z text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-006-0458-z text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lucchese G. Department of Biochemistry and Molecular Biology "Ernesto Quagliariello”, University of Bari, Bari, Italy aut NATIONALLICENCE 700 1- Stufano A. Department of Biochemistry and Molecular Biology "Ernesto Quagliariello”, University of Bari, Bari, Italy aut NATIONALLICENCE 700 1- Trost B. Department of Computer Science, University of Saskatchewan, Saskatoon, Canada aut NATIONALLICENCE 700 1- Kusalik A. Department of Computer Science, University of Saskatchewan, Saskatoon, Canada aut NATIONALLICENCE 700 1- Kanduc D. Department of Biochemistry and Molecular Biology "Ernesto Quagliariello”, University of Bari, Bari, Italy aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 33/4(2007-11-01), 703-707 0939-4451 33:4<703 2007 33 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer