The insect kinins are present in a wide variety of insects and function as potent diuretic peptides in flies. A C-terminal aldehyde insect kinin analog, Fmoc-RFFPWG-H (R-LK-CHO), demonstrates stimulation of Malpighian tubule fluid secretion in crickets, but shows inhibition of both in vitro and in vivo diuresis in the housefly. R-LK-CHO reduced the total amount of urine voided over 3 h from flies injected with 1 microL of distilled water by almost 50%. The analog not only inhibits stimulation of housefly fluid secretion by the native kinin Musdo-K, but also by thapsigargin, a SERCA inhibitor, and by ionomycin, a calcium ionophore. The activity of R-LK-CHO is selective, however, as related C-terminal aldehyde analogs do not demonstrate an inhibitory response on housefly fluid secretion. The selective inhibitory activity of R-LK-CHO on housefly tubules represents an important lead in the development of environmentally friendly insect management agents based on the insect kinins.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.peptides.2006.09.017 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Hydrodynamic characterization of the FtsZ protein from Escherichia coli demonstrates the presence of linear and lateral trimers.
Anal Biochem
April 2025
Laboratorio de Biología Estructural y Molecular BEM, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425 Ñuñoa, Santiago, 7800003, Chile; Laboratorio de Biotecnología Vegetal y Ambiental Aplicada, Universidad Tecnológica Metropolitana, Santiago, Chile.
FtsZ is a bacterial protein that plays a crucial role in cytokinesis by forming the Z-ring. This ring acts as a scaffold to recruit other division proteins and guide the synthesis of septal peptidoglycan, which leads to cell constriction. In its native state, the FtsZ protein from Escherichia coli (EcFtsZ) is a multi-oligomer comprising dimers, trimers, tetramers, and hexamers in a dynamic self-association equilibrium depending on its concentration.
View Article and Find Full Text PDFProtein stabilization in spray drying and solid-state storage by using a 'molecular lock' - exploiting bacterial adaptations for industrial applications.
RSC Chem Biol
December 2024
SSPC - The Science Foundation Ireland Research Centre for Pharmaceuticals, Department of Chemical Sciences, Bernal Institute, University of Limerick Limerick Ireland
Small, stable biomedicines, like peptides and hormones, are already available on the market as spray dried formulations, however large biomolecules like antibodies and therapeutic enzymes continue to pose stability issues during the process. Stresses during solid-state formation are a barrier to formulation of large biotherapeutics as dry powders. Here, we explore an alternative avenue to protein stabilisation during the spray drying process, moving away from the use of excipients.
View Article and Find Full Text PDFAn Enabling Peptide Ligation Induced by Thiol-Salicylaldehyde Ester for Chemical Protein Synthesis.
Adv Sci (Weinh)
December 2024
Department of Medicinal Chemistry, Key Laboratory of Chemical Biology (Ministry of Education), School of Pharmacy, Cheeloo College of Medicine, Shandong University, Jinan, Shandong, 250012, China.
Chemical protein synthesis by amide-forming ligation of two unprotected peptide segments offers an effective strategy for the preparation of protein derivatives that are not accessible through bioengineering approaches. Herein, an unprecedented chemical ligation between peptides with C-terminal 2-mercaptobenzaldehyde (thiol-salicylaldehyde, TSAL) esters and peptides bearing N-terminal cysteine/penicillamine is reported. Reactive peptide TSAL esters can be obtained from peptide hydrazides in an operationally simple and highly effective manner.
View Article and Find Full Text PDFAdvanced glycation end-product crosslinking activates a type VI secretion system phospholipase effector protein.
Nat Commun
October 2024
Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, Santa Barbara, 93106, USA.
Article Synopsis
- Advanced glycation end-products (AGE) are harmful protein modifications linked to serious health issues like neurodegenerative diseases, heart disease, and diabetes, caused by toxic byproducts of glucose metabolism.
- Research reveals that AGE crosslinking activates a specific antibacterial enzyme in the bacteria Enterobacter cloacae, which is linked through a unique interaction between two amino acids.
- The study highlights that glycation can stabilize protein structures, especially in environments where traditional stabilizing methods (like disulfide bonds) are not effective, suggesting broader implications for protein engineering.
Revealing reaction intermediates in one-carbon elongation by thiamine diphosphate/CoA-dependent enzyme family.
Commun Chem
July 2024
eBERlight and Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Lemont, IL, USA.
2-Hydroxyacyl-CoA lyase/synthase (HACL/S) is a thiamine diphosphate (ThDP)-dependent versatile enzyme originally discovered in the mammalian α-oxidation pathway. HACL/S natively cleaves 2-hydroxyacyl-CoAs and, in its reverse direction, condenses formyl-CoA with aldehydes or ketones. The one-carbon elongation biochemistry based on HACL/S has enabled the use of molecules derived from greenhouse gases as biomanufacturing feedstocks.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!