Active fragments and analogs of the insect neuropeptide leucopyrokinin: structure-function studies.

Abstract:

:Evaluation of analogs of the blocked insect myotropic neuropeptide leucopyrokinin (LPK) has demonstrated its relative insensitivity to amino acid substitution in the N-terminal in contrast to the C-terminal region. Truncated analogs of LPK without the first, second, and third N-terminal amino acids retain a significant 144%, 59% and 30% of the activity of the parent octapeptide, respectively. The [2-8]LPK analog is the first fragment of an insect neuropeptide to exhibit greater activity than the parent hormone. In contrast, truncated analogs of the insect myotropic, proctolin, exhibit little or no activity. The pentapeptide fragment Phe-Thr-Pro-Arg-Leu-NH2 has been identified as the active core of LPK.

authors

Nachman RJ,Holman GM,Cook BJ

doi

10.1016/0006-291x(86)90315-3

subject

Has Abstract

pub_date

1986-06-30 00:00:00

pages

936-42

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(86)90315-3

journal_volume

137

pub_type

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