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Volumn 15, Issue 44, 2009, Pages 11867-11877

Engineering a β-helical d,l-peptide for folding in polar media

Author keywords

Beta helix; Cyclic compounds; Foldamers; NMR spectroscopy; Peptides

Indexed keywords

ANALYTICAL ULTRACENTRIFUGATION; BIOPHYSICAL CHARACTERIZATION; CD SPECTRA; CYCLIC COMPOUNDS; FOLDAMERS; FUTURE DESIGNS; HELICAL PEPTIDE; HELICAL STRUCTURES; HYDROGEN BONDINGS; HYDROPHOBIC PEPTIDES; NMR SPECTROSCOPY; NON-POLAR SOLVENTS; POLAR MEDIA; POLAR RESIDUES; POLAR SOLVENTS; SPECTROSCOPIC DATA; STERIC CONSTRAINT; STRUCTURE CALCULATION; THERMAL MELTING; TWO-STATE;

EID: 72949107698     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.200901129     Document Type: Article
Times cited : (12)

References (123)
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    • note
    • For consistency, we used a PBS concentration of 1 mm both for high-concentration aqueous samples ('1 mm peptide 1), and for low-concentration aqueous samples (1 mm led to unacceptable absorbance in the far-UV CD spectra. Results from variable-concentration CD spectroscopy experiments (Figure 2) indicate that sample 1w has a similar conformation at 2.5 mm, where the PBS concentration was less than the peptide concentration, and at 0.1 mm, in which the PBS concentration was ten times the peptide concentration. Before beginning CD or NMR spectroscopy experiments, we checked the pH of each sample of 1w and found it to be 7; we attribute the stabilization of the sample pH at 7 to self-buffering by the peptide. We note, furthermore, that the CD spectra of samples in pure water were indistinguishable from those of samples in PBS.
  • 47
    • 72949107762 scopus 로고    scopus 로고
    • note
    • See the Supporting Information for details. We note that, in addition to variable concentration CD and analytical ultracentrifugation, other techniques exist for assessing the aggregation state of biomolecules, including a) gel filtration chromatography (see: Gel Filtration:Principles and Methods. Handbook 18-1022-18; Amersham Biosciencenes, Uppsala, 2002.), and
  • 48
    • 0000673856 scopus 로고
    • For simplicity, we refer to a b-hairpin and b-hairpin/b5.6 helix as a secondary and a supersecondary structure, respectively; we note, however, that b hairpins are sometimes considered supersecondary structures in their own right
    • For simplicity, we refer to a b-hairpin and b-hairpin/b5.6 helix as a secondary and a supersecondary structure, respectively; we note, however, that b hairpins are sometimes considered supersecondary structures in their own right.
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    • Morris, K.F.1    Johnson, C.S.2
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    • note
    • The coordinates for the energy-minimized average structure of 1m (Figure 7b) and those of the energy minimized average of the 10 lowest-energy structures for 1w (Figure 7c) have been deposited in the BioMagResBank: http://www.bmrb.wisc.edu/(BMRB ID 15 748 and 15749, respectively.).
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    • 29144433298 scopus 로고    scopus 로고
    • To avoid confusion, we refer to the unfolded forms of foldamers as having only primary structure. We note, however, that, at least for peptides and proteins composed of a-amino acid residues, growing experimental evidence suggests that the unfolded states are not true random coils and instead possess at least nascent secondary structure. See, for example: Z. S. Shi, K. Chen, Z. G. Liu, A. Ng, W. C. Bracken, N. R. Kallenbach, Proc. Natl. Acad. Sci. USA 2005, 102, 17964-17968.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17964-17968
    • Shi, Z.S.1    Chen, K.2    Liu, Z.G.3    Ng, A.4    Bracken, W.C.5    Kallenbach, N.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.