Purification and characterization of antimicrobial peptides from the skin of the North American green frog Rana clamitans☆

Halverson, Thomas; Basir, Yousef J.; Knoop, Floyd C.; Conlon, J. Michael

doi:10.1016/s0196-9781(00)00178-9

Cited by 73 publications

(35 citation statements)

References 17 publications

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“…Moreover, a similar peptide was recently isolated from another frog species, namely alyteserin-2 from the midwife toad Alytes obstetricans (Conlon et al 2009). In this search, additional peptides were retrieved, namely several ranalexins, temporins 1DYa and PTa and brevenins 1PTa and 1PTb from diverse Rana species (Halverson et al 2000; Conlon et al 2008), hylin a1 from the spotted treefrog ( Hypsiboas albopunctatus ) (Castro et al 2009) as well as kassorin S from the African hyperoliid frog ( Kassina senegalensis ) (Chen et al 2010) and signiferin-2 from an Australian froglet ( Crinia signifera ) (Maselli et al 2004). All of these are predicted to be good substrates for the Bombina isomerase.…”

Section: Resultsmentioning

confidence: 99%

Substrate specificity of a peptidyl-aminoacyl-l/d-isomerase from frog skin

et al. 2011

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In the skin of fire-bellied toads (Bombina species), an aminoacyl-l/d-isomerase activity is present which catalyses the post-translational isomerization of the l- to the d-form of the second residue of its substrate peptides. Previously, this new type of enzyme was studied in some detail and genes potentially coding for similar polypeptides were found to exist in several vertebrate species including man. Here, we present our studies to the substrate specificity of this isomerase using fluorescence-labeled variants of the natural substrate bombinin H with different amino acids at positions 1, 2 or 3. Surprisingly, this enzyme has a rather low selectivity for residues at position 2 where the change of chirality at the alpha-carbon takes place. In contrast, a hydrophobic amino acid at position 1 and a small one at position 3 of the substrate are essential. Interestingly, some peptides containing a Phe at position 3 also were substrates. Furthermore, we investigated the role of the amino-terminus for substrate recognition. In view of the rather broad specificity of the frog isomerase, we made a databank search for potential substrates of such an enzyme. Indeed, numerous peptides of amphibia and mammals were found which fulfill the requirements determined in this study. Expression of isomerases with similar characteristics in other species can therefore be expected to catalyze the formation of peptides containing d-amino acids.Electronic supplementary materialThe online version of this article (doi:10.1007/s00726-011-0890-6) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Substrate specificity of a peptidyl-aminoacyl-l/d-isomerase from frog skin

et al. 2011

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“…To keep up with the growing demand, AMPs purification methods must be developed to be efficient, reliable and cost effective. Although a variety purification schemes have been described for AMPs (Gomes et al, 2005;Halverson, Basir, Knoop, & Michael Conlon, 2000;Lee et al, 1999;Liepke, Zucht, Forssmann, & Ständ-ker, 2001;Ovchinnikova et al, 2004), these isolation methods require multiple steps to produce highly-purified AMPs, resulting in undesirable losses of the already limited material. Thus, the discovery of improved purification methods is a driving force for our research into further application of AMPs.…”

Section: Introductionmentioning

confidence: 99%

Discovery of a novel antimicrobial peptide using membrane binding-based approach

et al. 2009

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“…Temporins are short (13-residue) peptides, with an amidated C terminus and with only one positively charged amino acid. They were first identified in R. temporaria skin secretions (31) and further detected in several North American Rana species, such as Rana clamitans (32), Rana luteiventris (33), Rana pipiens (33), and Rana grylio (34). Temporins, together with indolicidin, are among the smallest AMPs isolated so far from animal sources.…”

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confidence: 99%