2013
DOI: 10.1016/j.jprot.2012.09.016
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The chains of the heterodimeric amphibian skin antimicrobial peptide, distinctin, are encoded by separate messenger RNAs

Abstract: Verhaert, P. (2013). The chains of the heterodimeric amphibian skin antimicrobial peptide, distinctin, are encoded by separate messenger RNAs.

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Cited by 9 publications
(7 citation statements)
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“…They are also present in the skin secretions of frogs, such as some AMPs from Rana spp., which contain a disulphide-bridged cyclic domain of varying size (six or seven residues; the “Rana box” Conlon, 2011 ) and the Bowman-Birk inhibitor (BBI) like peptides, which contain a canonical disulphide BBI loop with 11 residues (Song et al, 2008 ). However, in all these cases, the disulphide bridge is intramolecular, whereas the bridge in distinctin is found between the heterodimers, with each chain being encoded by separate mRNAs (Evaristo et al, 2013 ) as well as having distinct physiochemical properties, albeit not as extreme as we found for the two domains of DLP-PH. The resemblance between DLP-PH and distinctin is further strengthened by the extremely high degree of similarity between the primary structures of the N-terminal domain of DLP-PH and the B-chain of distinctin.…”
Section: Discussionsupporting
confidence: 44%
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“…They are also present in the skin secretions of frogs, such as some AMPs from Rana spp., which contain a disulphide-bridged cyclic domain of varying size (six or seven residues; the “Rana box” Conlon, 2011 ) and the Bowman-Birk inhibitor (BBI) like peptides, which contain a canonical disulphide BBI loop with 11 residues (Song et al, 2008 ). However, in all these cases, the disulphide bridge is intramolecular, whereas the bridge in distinctin is found between the heterodimers, with each chain being encoded by separate mRNAs (Evaristo et al, 2013 ) as well as having distinct physiochemical properties, albeit not as extreme as we found for the two domains of DLP-PH. The resemblance between DLP-PH and distinctin is further strengthened by the extremely high degree of similarity between the primary structures of the N-terminal domain of DLP-PH and the B-chain of distinctin.…”
Section: Discussionsupporting
confidence: 44%
“…: Q17UZ0 ). Additionally, the DLP-PH peptide precursor demonstrated strong similarity to the B-chain peptide (distinctin-B) precursor of the heterodimeric AMP distinctin from Phyllomedusa distincta (Batista et al, 2001 ; Evaristo et al, 2013 ) along most of the entire precursor-encoding cDNA of the latter. Noticeable dissimilarity only arose in the C-terminal domain of the mature peptides, with DLP-PH also being much longer than distinctin-B (Figures 1B,C ).…”
Section: Resultsmentioning
confidence: 99%
“…Such behavior is difficult to predict and appears to be unique to certain complementary sequences with the required structural information to exclude the formation of undesired connectivities. In other cases, such as that of the single‐disulfide‐bonded distinctin, aerial oxidation of the two peptide chains resulted in a mixture of products and thus required directed disulfide‐bond formation to achieve the correct pairing . Members of the insulin superfamily further illustrate this variability, where minor changes to the sequence may have detrimental effects on the heterodimerization process…”
Section: Figurementioning
confidence: 99%
“…[10] Such behavior is difficult to predict and appears to be unique to certain complementary sequences with the required structural information to exclude the formation of undesired connectivities. In other cases,s uch as that of the single-disulfide-bonded distinctin, aerial oxidation of the two peptide chains resulted in am ixture of products [11] and thus required directed disulfide-bond formation to achieve the correct pairing. [12] Members of the insulin superfamily further illustrate this variability,w here minor changes to the sequence may have detrimental effects on the heterodimerization process.…”
Section: In Memory Of Dianne Alewoodmentioning
confidence: 99%