Isolation of achatin-i, a neuroactive tetrapeptide having a d-phenylalanine residue, from Achatina ganglia, and its effects on Achatina giant neurones

Kamatani, Yoshimi; Minakata, Hiroyuki; Nomoto, Kyosuke; Hwi, Kim Kah; Yongsiri, Anchalee; Takeuchi, Hiroshi

doi:10.1016/0742-8413(91)90186-w

Cited by 10 publications

References 12 publications

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Folding propensity and biological activity of peptides: The effect of a single stereochemical isomerization on the conformational properties of bombinins in aqueous solution

Bozzi¹,

Mangoni

Rinaldi

et al. 2008

Biopolymers

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Folding propensities of bombinins H2 and H4, two members of amphibian bombinins H, a family of 17-20 residue alpha-helical peptides, have been investigated by means of circular dichroism (CD) measurements and molecular dynamics (MD) simulations. The two peptides, with primary structure IIGPVLGLVGSALGGLLKKI-NH2 and differing only for the configuration of the second aminoacid (an L-isoleucine in H2 and a D-alloisoleucine in H4) behave rather differently in solution. In particular both CD measurements and MD simulations indicate that bombinin H2 shows a markedly higher tendency to fold. From a careful inspection of MD trajectories it emerges that the stereochemical isomerization mutation of residue 2 to D-alloisoleucine in H4 peptide, drastically decreases its ability to form intrapeptide contacts. MD simulations also indicate that the conformational sampling in both systems derives from a subtle combination of energetic and entropic effects both involving the peptide itself and the solvent. The present results have been finally paralleled with preliminary information on bombinins H2 and H4 biological activity, i.e. interaction with membrane, supporting the hypothesis of an "already folded" conformation in water rather than interfacial folding tenet.

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Folding propensity and biological activity of peptides: The effect of a single stereochemical isomerization on the conformational properties of bombinins in aqueous solution

Bozzi¹,

Mangoni

Rinaldi

et al. 2008

Biopolymers

View full text Add to dashboard Cite

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Natural Occurrence and Industrial Applications of d‐Amino Acids: An Overview

Martínez‐Rodríguez

Martínez-Gómez

Rodríguez‐Vico

et al. 2010

Chemistry & Biodiversity

115

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Interest in D-amino acids has increased in recent decades with the development of new analytical methods highlighting their presence in all kingdoms of life. Their involvement in physiological functions, and the presence of metabolic routes for their synthesis and degradation have been shown. Furthermore, D-amino acids are gaining considerable importance in the pharmaceutical industry. The immense amount of information scattered throughout the literature makes it difficult to achieve a general overview of their applications. This review summarizes the state-of-the-art on D-amino acid applications and occurrence, providing both established and neophyte researchers with a comprehensive introduction to this topic.

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The effect of proctolin analogues and other peptides on locust oviduct muscle contractions

1993

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Isolation of achatin-i, a neuroactive tetrapeptide having a d-phenylalanine residue, from Achatina ganglia, and its effects on Achatina giant neurones

Cited by 10 publications

References 12 publications

Folding propensity and biological activity of peptides: The effect of a single stereochemical isomerization on the conformational properties of bombinins in aqueous solution

Folding propensity and biological activity of peptides: The effect of a single stereochemical isomerization on the conformational properties of bombinins in aqueous solution

Natural Occurrence and Industrial Applications of d‐Amino Acids: An Overview

The effect of proctolin analogues and other peptides on locust oviduct muscle contractions

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