If you are experiencing problems downloading PDF or HTML fulltext, our helpdesk recommend clearing your browser cache and trying again. If you need help in clearing your cache, please click here . Still need help? Email firstname.lastname@example.org
Series of eight new monocyclic analogues of trypsin inhibitor SFTI-1 was synthesized by the solid phase method. In these analogues disulfide bridge Cys3 — Cys11 present in native inhibitor was replaced by different-sized carbonyl bridges formed by the amino groups of the side chain of Lys, Orn, Dab or Dap located in positions 3 and/or 11. All analogues appeared to be potent trypsin inhibitors. The values of association equilibrium constants determined with bovine β-trypsin ranging 108 — 109 M-1 with the highest (3.90 x 109 M-1) determined for analogue containing Lys and Dap in aforementioned positions. The obtained results clearly shown that this redox stable modification is well tolerated in the structure of proteinase inhibitor. It is worth stressing that the procedure of the introduction of carbonyl bridge into the peptide structure is straightforward and therefore beneficial for the design of new enzyme inhibitors.
Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.