Abstract
The collagen-tailed form of acetylcholinesterase (AChE) binds to heparin and heparan sulfate proteoglycans. We have employed synthetic peptides corresponding to the central collagenic region of the tail of AChE, to identify the heparin-binding domains of the tail of asymmetric AChE. Two putative heparin-binding consensus sequences were localized in the collagenic tail. Peptides containing such sequences (P-(145-159) and P-(249-262)) were able to release asymmetric AChE bound to heparin-agarose. A triple mutation, Asn-Asp-Gly-Gly instead of Arg-His-Gly-Arg, completely abolishes the capacity of the peptide P-(145-159) to elute AChE from the heparin column. Our results suggest that the interaction between the collagen-tailed AChE and proteoglycans is mediated by clusters of basic residues that form two belts around the triple helix of the collagenic tail.
Highlights
I.) and a Research Assistantship from DIUC
In the present work we demonstrate that synthetic peptides, containing heparin-binding consensus sequences present in the tail of asymmetric AChE, released the collagen-tailed AChE previously bound to heparin-agarose
The results were obtained with peptides synthesized following the corresponding sequences of the two heparin-binding consensus sequences localized near the N-terminal domain, residues 145-159, and the C-terminaI domain, residues 249262 (after Krejci et ai. [5]), of the collagenic tail and suggest that two specific regions of the collagenic region of the tail of asymmetric AChE are relevant for the protein-GAG interaction
Summary
I.) and a Research Assistantship from DIUC Features of protein structure that control heparin binding have been partially elucidated by studying the heparin binding properties of protein fragments, synthetic peptides, and chemically modified proteins [13,14,15]. Such studies have led to the identification of putative heparin-binding consensus sequences, including sequences like -B-B-X-B- and -B-B-B-X-XB-, where B represents a basic residue and X a hydropathic residue [16,17]. Synthetic peptides containing the sequences of such domains, but not a mutant peptide lacking it, are able to detach asymmetric AChE bound to heparin-agarose
Sign-in/Register to view highlights & summary 
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
