b-Amino Acid Analogs of an Insect Neuropeptide Feature Potent Bioactivity and Resistance to Peptidase Hydrolysis
نویسندگان
چکیده
Bioactivity and Resistance to Peptidase Hydrolysis Pawel Zubrzak, Howard Williams, Geoffrey M. Coast, R. Elwyn Isaac, Gloria Reyes-Rangel, Eusebio Juaristi, Janusz Zabrocki, Ronald J. Nachman 1 Areawide Pest Management Research Unit, Southern Plains Agricultural Research Center, U.S. Department of Agriculture, 2881 F/B Road, College Station, TX 2 Department of Chemistry, Texas A&M University, College Station, TX 77843 3 School of Biological and Chemical Sciences, Birkbeck College, London, WC1E 7HX, United Kingdom 4 Faculty of Biological Sciences, University of Leeds, Clarendon Way, Leeds LS2 9JT, United Kingdom 5 Department of Chemistry, Centro de Investigacion y de Estudios Avanzados del IPN, Mexico D.F. 6 Institute of Organic Chemistry, Technical University of Lodz, Zeromskiego 116, 90-924 Lodz, Poland
منابع مشابه
Beta-amino acid analogs of an insect neuropeptide feature potent bioactivity and resistance to peptidase hydrolysis.
Insect neuropeptides of the insect kinin class share a common C-terminal pentapeptide sequence F(1)X(1)(2)X(2)(3)W(4)G(5)-NH(2) (X(2)(3) = P, S, A) and regulate such critical physiological processes as water balance and digestive enzyme release. Analogs of the insect kinin class, in which the critical residues of F(1), P(3), and W(4) were replaced with beta(3)-amino acid or their beta(2)-homo-a...
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The multifunctional arthropod 'insect kinins' share the evolutionarily conserved C-terminal pentapeptide motif Phe-X(1)-X(2)-Trp-Gly-NH(2), where X(1)=His, Asn, Ser, or Tyr and X(2)=Ser, Pro, or Ala. Insect kinins regulate diuresis in many species of insects. Compounds with similar biological activity could be exploited for the control of arthropod pest populations such as the mosquito Aedes ae...
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