Design and synthesis of novel nonpolar host peptides for the determination of the 310- and α-helix compatibilities of α-amino acid buildig blocks: An assessment of α,α-disubstituted glycines

Obrecht, Daniel; Altorfer, Michael; Bohdal, Udo; Daly, J. J.; Huber, Walter; Labhardt, Alexander M.; Lehmann, Christian W.; Müller, Klaus; Ruffieux, Ruth; Schönholzer, Peter; Spiegler, Clive; Zumbrunn, Cornelia

doi:10.1002/(sici)1097-0282(19971015)42:5<575::aid-bip7>3.0.co;2-n

Cited by 25 publications

(2 citation statements)

References 82 publications

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“…In Fig. 2 we show a series of spectra corresponding to f H = 0.0, 0.2, 0.4, 0.6, 0.8 and 1.0 using reported K-helix and coil base spectra [16]. As can be seen from Fig.…”

Section: Studiesmentioning

confidence: 95%

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Direct evidence for alteration of unfolding profile of a helical peptide by far‐ultraviolet circular dichroism aromatic side‐chain contribution

Banerjee

Basu

2002

FEBS Letters

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Aromatic side-chains are known to contribute to the far-UV circular dichroism (CD) spectra of peptides and proteins. Among other things, this can signi¢cantly a¡ect the measured helix propensities of amino acids [Chakrabartty et al., Biochemistry 32 (1993) 5560^5565]. In order to address how interfering side-chain contributions can a¡ect the backbone unfolding transition of a helical peptide, as monitored by [a a] 222 (molar ellipticity at 222 nm), we have studied the unfolding transition of a short designed (K K-amino isobutyric acid/alanine-based) helical peptide containing an interacting Tyr residue. The guanidinium hydrochloride-induced unfolding of the peptide, as monitored by [a a] 222 , showed the presence of a sharp transition superposed over a much broader transition. When the same experiment was performed with a similar peptide that lacked the interacting Tyr residue, the sharp transition disappeared and only the broad transition remained. The sharp transition was assigned to originate from the interacting Tyr sidechain. This demonstrates that conformationally restricted aromatic side-chains that interact with the helical backbone not only can alter the backbone far-UV CD signal, they may also alter the unfolding pro¢les, monitored by far-UV CD, rendering them un¢t for a simple analysis for extracting the appropriate unfolding thermodynamic parameters. ß

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“…In Fig. 2 we show a series of spectra corresponding to f H = 0.0, 0.2, 0.4, 0.6, 0.8 and 1.0 using reported K-helix and coil base spectra [16]. As can be seen from Fig.…”

Section: Studiesmentioning

confidence: 95%

“…The far-UV CD spectra of a polypeptide backbone generated as a function of fraction helicity (f H ) in a two-state model (helix and coil) using base spectra reported by Obrecht et al[16]. The characteristic ZZ* e minimum, corresponding to the helix, begins to appear beyond 203 nm only at greater than 30% f H values.…”

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confidence: 99%

Direct evidence for alteration of unfolding profile of a helical peptide by far‐ultraviolet circular dichroism aromatic side‐chain contribution

Banerjee

Basu

2002

FEBS Letters

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N-[(Dimethylamino)[(2-oxo-1(2H)-pyridinyl)oxy]methylene]-N-methylmethanaminium tetrafluoroborate

Goodreid

Batey

2016

Encyclopedia of Reagents for Organic Synthesis

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Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

et al. 2001

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The preferred conformations of peptides heavily based on the currently extensively exploited achiral and chiral α‐amino acids with a quaternary α‐carbon atom, as determined by conformational energy computations, crystal‐state (x‐ray diffraction) analyses, and solution (1H‐NMR and spectroscopic) investigations, are reviewed. It is concluded that 310/α‐helical structures and the fully extended (C5) conformation are preferentially adopted by peptide sequences characterized by this family of amino acids, depending upon overall bulkiness and nature (e.g., whether acyclic or C αi ↔ C αitalici cyclized) of their side chains. The intriguing relationship between α‐carbon chirality and bend/helix handedness is also illustrated. γ‐Bends and semiextended conformations are rarely observed. Formation of β‐sheet structures is prevented. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 60: 396–419, 2001

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Design and synthesis of novel nonpolar host peptides for the determination of the 310- and α-helix compatibilities of α-amino acid buildig blocks: An assessment of α,α-disubstituted glycines

Cited by 25 publications

References 82 publications

Direct evidence for alteration of unfolding profile of a helical peptide by far‐ultraviolet circular dichroism aromatic side‐chain contribution

Direct evidence for alteration of unfolding profile of a helical peptide by far‐ultraviolet circular dichroism aromatic side‐chain contribution

N-[(Dimethylamino)[(2-oxo-1(2H)-pyridinyl)oxy]methylene]-N-methylmethanaminium tetrafluoroborate

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

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