tailieunhanh - Báo cáo khoa học: A search for synthetic peptides that inhibit soluble N-ethylmaleimide sensitive-factor attachment receptor-mediated membrane fusion

Soluble N-ethylmaleimide sensitive-factor attachment receptor (SNARE) proteins have crucial roles in driving exocytic membrane fusion. Molecular recognition between vesicle-associated (v)-SNARE and target membrane (t)-SNARE leads to the formation of a four-helix bundle, which facilitates the merging of two apposing membranes. | ỊFEBS Journal A search for synthetic peptides that inhibit soluble N-ethylmaleimide sensitive-factor attachment receptor-mediated membrane fusion Chang H. Jung1 z Yoo-Soo Yang1 z Jun-Seob Kim1 Jae-Il Shin1 Yong-Su Jin1 Jae Y. Shin1 Jong H. Lee2 Koo M. Chung2 Jae S. Hwang3 Jung M. Oh1 Yeon-Kyun Shin4 and Dae-Hyuk Kweon1 1 Schoolof Biotechnology and Bioengineering Sungkyunkwan University Gyeonggi-do Korea 2 Schoolof Bioresource Sciences Andong NationalUniversity Gyeongsangbuk-do Korea 3 Amorepacific R D Center Yongin Korea 4 Department of Biochemistry Biophysics and Molecular Biology Iowa State University Ames IA USA Keywords exocytosis membrane fusion neurotransmitter release SNARE SNARE-patterned peptide Correspondence . Kweon Schoolof Biotechnology and Bioengineering Sungkyunkwan University Suwon Gyeonggi-do 440-746 Korea Fax 82 31 290 7870 Tel 82 31 290 7869 E-mail dhkweon@ These authors contributed equally to this work Received 28 December 2007 revised 9 March 2008 accepted 10 April 2008 doi Soluble N-ethylmaleimide sensitive-factor attachment receptor SNARE proteins have crucial roles in driving exocytic membrane fusion. Molecular recognition between vesicle-associated v -SNARE and target membrane t -SNARE leads to the formation of a four-helix bundle which facilitates the merging of two apposing membranes. Synthetic peptides patterned after the SNARE motifs are predicted to block SNARE complex formation by competing with the parental SNAREs inhibiting neuronal exocytosis. As an initial attempt to identify the peptide sequences that block SNARE assembly and membrane fusion we created thirteen 17-residue synthetic peptides derived from the SNARE motifs of v- and t-SNAREs. The effects of these peptides on SNARE-mediated membrane fusion were investigated using an in vitro lipid-mixing assay in vivo neurotransmitter release and SNARE complex formation assays in PC12 cells. Peptides derived from the N-terminal region of .

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