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α-Amanitin Bacitracin Ciclosporin. Cyclic peptides are polypeptide chains which contain a circular sequence of bonds. [1] This can be through a connection between the amino and carboxyl ends of the peptide, for example in cyclosporin; a connection between the amino end and a side chain, for example in bacitracin; the carboxyl end and a side chain, for example in colistin; or two side chains ...
Cyclotides have a well-defined three-dimensional structure due to their interlocking disulfide bonds and cyclic peptide backbone. Backbone loops and selected residues are labeled on the structure to help orientation. The amino acid sequence (single-letter amino acid representation) for this peptide is indicated on the sequence diagram to the right.
A number of natural antimicrobial peptides are cyclic, and the products of SICLOPPS are "increasingly viewed as ideal backbones for modulation of protein-protein interactions." [3] Circular peptides tend to be resistant to protease activity, and may be suitable for use as orally administered drugs.
Crystal structure of an extracellular segment of integrin alphaVbeta3 complexed with a cyclic peptide containing the arginyl-glycyl-aspartic acid (RGD) sequence. RGD is shown in maroon. CEND-1, also known as iRGD, is a cyclic peptide that homes to tumors via binding to integrin alpha V receptors. [22]
Lin and her lab use computational chemistry to provide information on the solution structures of cyclic peptides. [2] They recently successfully used molecular dynamics simulation with enhanced sampling methods to design well-structured cyclic peptides. [12] [13]
As of February 2012, the Circular Permutation Database [8] contains 2,238 circularly permuted protein pairs with known structures, and many more are known without structures. [9] The CyBase database collects proteins that are cyclic, some of which are permuted variants of cyclic wild-type proteins. [10]
The ICK motif is a very stable protein structure which is resistant to heat denaturation and proteolysis. [6] CK peptide components of venoms target voltage-gated ion channels but members of the family also act as antibacterial and haemolytic agents. [7] Plant ICK proteins are often protease inhibitors.
Each nonribosomal peptide synthetase can synthesize only one type of peptide. Nonribosomal peptides often have cyclic and/or branched structures, can contain non-proteinogenic amino acids including D-amino acids, carry modifications like N-methyl and N-formyl groups, or are glycosylated, acylated, halogenated, or hydroxylated.