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제120회 대한화학회 학술발표회, 총회 및 기기전시회 Enzymatic crosslinking of side chains generates a modified peptide, Plesiocin, with four hairpin-like bicyclic repeats [TCI 포스터상]

등록일
2017년 8월 24일 16시 51분 38초
접수번호
2089
발표코드
BIO.P-277 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 19일 (목요일) 11:00~12:30
발표형식
포스터
발표분야
Life Chemistry
저자 및
공동저자
hyunbin lee, Seokhee Kim1,*
Chemistry, Seoul National University, Korea
1Division of Chemistry, Seoul National University, Korea
Ribosomally synthesized and Post-translationally modified Peptides represents a unique class in natural products. Especially, macrocyclization involved in RiPP biosynthesis yields topologically diverse cyclic peptides. Cyclization via ester or amide bonds are easily found in RiPP, but crosslinking of two side chains through ester or amide is uniquely found in the microviridin class of natural products with a single consensus sequence of peptides. Here, we report plesiocin, a new microviridin-like RiPP which has a distinct sequence pattern, also can be enzymatically crosslinked via ester bonds to make a novel modified peptide, and showed strong inhibitory effect against some serine proteases. A single ATP-grasp enzyme binds to a leader peptide, of which only 13 residues are required for binding, and performs eight esterification reactions on the core peptide. We demonstrate that connectivity of side chains can be easily analyzed by the combination of tandem mass spectrometry and methanolysis of esters. We suggest that crosslinking of peptide side chains can generate diverse structure.

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