| hv-bbi--a novel amphibian skin bowman-birk-like trypsin inhibitor. | here we describe the isolation of a novel c-terminally amidated octadecapeptide--svigcwtksipprpcfvk-amide--that contains a disulphide loop between cys(5) and cys(15) that is consistent with a bowman-birk type protease inhibitor, from the skin secretion of the chinese bamboo odorous frog, huia versabilis. named hv-bbi, the peptide is encoded by a single precursor of 62 amino acid residues whose primary structure was deduced from cloned skin cdna. the precursor exhibits the typical organization of ... | 2008 | 18486596 |
| a novel kunitzin-like trypsin inhibitor isolated from defensive skin secretion of odorrana versabilis. | protease inhibitors that were identified from amphibian skin secretions with low molecular weights and potent inhibitory activity were thought to be potential candidates for novel peptide drugs. here, a novel peptide with trypsin inhibitory activity was found in the skin secretion of the chinese bamboo leaf odorous frog, odorrana versabilis. based on the sequence alignments of sequencing results, the novel peptide (alkypfrckaafc) was named as kunitzin-ov. the synthetic replicate of kunitzin-ov w ... | 2019 | 31261722 |
| truncation of huia versabilis bowman-birk inhibitor increases its selectivity, matriptase-1 inhibitory activity and proteolytic stability. | a gradual truncation of the primary structure of frog skin-derived huia versabilis bowman-birk peptidic inhibitor (hv-bbi) resulted in 18-times stronger inhibitor of matriptase-1 (peptide 6, ki = 8 nm) in comparison to the full-length hv-bbi (ki = 155 nm). analogous increase in the inhibitory activity in correlation with the peptide length reduction was not observed in case of other serine proteases, bovine trypsin (ki = 151 nm for peptide 6 and ki = 120 nm for hv-bbi) and plasmin (ki = 120 nm f ... | 2020 | 32169666 |
| rapid identification of precursor cdnas encoding five structural classes of antimicrobial peptides from pickerel frog (rana palustris) skin secretion by single step "shotgun" cloning. | the skin secretion of the north american pickerel frog (rana palustris) has long been known to have pronounced noxious/toxic properties and to be highly effective in defence against predators and against other sympatric amphibians. as it consists largely of a complex mixture of peptides, it has been subjected to systematic peptidomic study but there has been little focus on molecular cloning of peptide-encoding cdnas and by deduction, the biosynthetic precursors that they encode. here, we demons ... | 2007 | 17698247 |
| the chinese bamboo leaf odorous frog (rana (odorrana) versabilis) and north american rana frogs share the same families of skin antimicrobial peptides. | the chinese bamboo leaf odorous frog (rana (odorrana) versabilis) and the north american pickerel frog (rana palustris) occupy different ecological niches on two different continents with no overlap in geographical distribution. r. palustris skin secretions contain a formidable array of antimicrobial peptides including homologs of brevinin-1, esculentin-1, esculentin-2, ranatuerin-2, a temporin and a family of peptides considered of unique structural attributes when isolated, palustrins 1-3. her ... | 2006 | 16621152 |
| cloning from tissue surrogates: antimicrobial peptide (esculentin) cdnas from the defensive skin secretions of chinese ranid frogs. | the defensive skin secretions of amphibians are a rich source of bioactive peptides. here we describe a rapid technique for skin granular gland transcriptome cloning from a surrogate tissue-the secretion itself. cdna libraries were constructed from lyophilized skin secretion from each of the chinese frogs (rana schmackeri, rana versabilis, and rana plancyi fukienensis) using magnetic oligo(dt) bead-captured polyadenylated mrna as templates. specific esculentin cdnas were amplified by 3'-race usi ... | 2006 | 16427248 |
| amphibian skin peptides and their corresponding cdnas from single lyophilized secretion samples: identification of novel brevinins from three species of chinese frogs. | brevinins are peptides of 24 amino acid residues, originally isolated from the skin of the oriental frog, rana brevipoda porsa, by nature of their microbicidal activity against a wide range of gram-positive and gram-negative bacteria and against strains of pathogenic fungi. cdna libraries were constructed from lyophilized skin secretion of three, unstudied species of chinese frog, odorrana schmackeri, odorrana versabilis and pelophylax plancyi fukienensis, using our recently developed technique. ... | 2006 | 16139929 |
| ornithokinin (avian bradykinin) from the skin of the chinese bamboo odorous frog, odorrana versabilis. | one of the most widespread and abundant families of pharmacologically active peptides in amphibian defensive skin secretions is the bradykinins and related peptides. despite retaining certain primary structural attributes that assign them to this peptide family, bradykinins and related peptides are unique among amphibian skin peptides in that they exhibit a wide range of primary structural variations, post-translational modifications and/or n-terminal or c-terminal extensions. initially it was b ... | 2014 | 24771465 |
| atomic resolution crystal structure of hv-bbi protease inhibitor from amphibian skin in complex with bovine trypsin. | protease inhibitors of the bowman-birk (bbi) family are commonly found in plants and animals where they play a protective role against invading pathogens. here, we report an atomic resolution (1å) crystal structure of a peptide inhibitor isolated from a skin secretion of a chinese bamboo odorous frog huia versabilis (hv-bbi) in complex with trypsin. hv-bbi shares significant similarities in sequence with a previously described inhibitor from a diskless-fingered odorous frog odorrana graham (orb) ... | 2015 | 25546528 |