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Volumn 11, Issue 6, 2007, Pages 685-692

Sophistication of foldamer form and function in vitro and in vivo

Author keywords

[No Author keywords available]

Indexed keywords

CELL PENETRATING PEPTIDE; PENETRATIN; PEPTIDE DERIVATIVE; PEPTOID; PROTEIN P53; SCAFFOLD PROTEIN;

EID: 36549088592     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2007.09.009     Document Type: Review
Times cited : (133)

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    • 9 adopts a unique, hydrogen bond facilitated threaded-loop conformation in acetontrile, exemplifying the ability of peptoids to adopt complex three-dimensional structures.
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    • Gorske B.C., and Blackwell H.E. Tuning peptoid secondary structure with pentafluoroaromatic functionality: A new design paradigm for the construction of discretely folded peptoid structures. J. Am. Chem. Soc. 128 (2006) 14378-14387. This work explored the role of pentafluoroaromatic side-chains in favoring peptoid helicity by destabilizing backbone hydrogen bonds. The ability to of this group to enhance π-stacking was dismissed in favor of its effect on backbone electrostatics.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.