Structural and conformational properties of (Z)-?-(1-naphthyl)- dehydroalanine residue

Inai, Yoshihito; Oshikawa, Tatsuo; Yamashita, Mitsuji; Hirabayashi, Tadamichi; Hirako, Takeshi

doi:10.1002/1097-0282(200101)58:1<9::aid-bip20>3.0.co;2-9

Cited by 17 publications

(21 citation statements)

References 49 publications

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“…15 Hexapeptide Boc-(L-Ala-⌬ Z Nap-LLeu) 2 -OMe (n ϭ 2 in Scheme 2) takes a 3 10 -helical structure, but partially contains an extended structure in solution. 14 The present work reveals whether the nona-and dodecapeptides (n ϭ 3 and 4), which contain three and four bulky naphthyl dehydroalanine residues, take predominantly a helical conformation or adopt another one.…”

Section: Introductionmentioning

confidence: 75%

“…⌬ Z Nap-Leu) 2 -OMe in a similar manner to the preparation of peptide n ϭ 2. 14 Boc-(Ala-⌬ Z Nap-Leu) 4 -OMe. Boc-Ala-⌬ Z NapLeu-OH was coupled with HCOOH ⅐ H-(Ala-⌬ Z Nap-Leu) 3 -OMe in a similar manner to the preparation of peptide nϭ2.…”

Section: Peptide Synthesismentioning

confidence: 99%

“…29 The ECEPP parameters of ⌬ Z Nap residue were determined in the previous study. 14 The program PEP-CON 30,31 for a conformational energy calculation and graphics of a given peptide was modified to be applicable to ␤-aryldehyroalanine-containing peptides. [32][33][34][35] The stepwise elongation 36,37 of the repeating unit -(Ala-⌬ Z Nap-Leu)-was used to find the stable conformations from all possible candidates.…”

Section: Conformational Energy Calculationsmentioning

confidence: 99%

“…14,15 Extensive conformational studies have been reported on dehydroresidues corresponding to conventional saturated residues, i.e., ⌬ Z Phe, 6 -9,16 -18 Z-dehydroleucine, 19,20 Z-dehydrovaline, 21,22 dehydroalanine, [23][24][25][26][27] and so on. However, little is known about the conformational preference in dehydroresidues having a ␤-substituent larger than phenyl group, although the preference should be affected by the size of ␤-substituent in dehydroresidue.…”

Section: Introductionmentioning

confidence: 99%

“…Understanding the effect of the ␤-substituent on the conformational preference in dehydroresidue is important when designing a novel molecular frame for arranging a wide variety of functional ␤-substituents of dehydropeptides. Tripeptide possessing a ⌬ Z Nap residue in the second position forms a type II ␤-turn in the solid state 14 and in solution. 15 Hexapeptide Boc-(L-Ala-⌬ Z Nap-LLeu) 2 -OMe (n ϭ 2 in Scheme 2) takes a 3 10 -helical structure, but partially contains an extended structure in solution.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

A helical arrangement of ?-substituents of dehydropeptides: Synthesis and conformational study of sequential nona- and dodecapeptides possessing (Z)-?-(1-naphthyl)dehydroalanine residues

Inai

Hirabayashi

2001

Biopolymers

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Section: Introductionmentioning

confidence: 75%

Section: Peptide Synthesismentioning

confidence: 99%

Section: Conformational Energy Calculationsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

A helical arrangement of ?-substituents of dehydropeptides: Synthesis and conformational study of sequential nona- and dodecapeptides possessing (Z)-?-(1-naphthyl)dehydroalanine residues

Inai

Hirabayashi

2001

Biopolymers

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Crystal structure of achiral nonapeptide Boc–(Aib–Δ^zPhe)₄–Aib–OMe at atomic resolution: Evidence for a 3₁₀‐helix

et al. 2003

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An x-ray crystallographic analysis was carried out for Boc-(Aib-DeltaZPhe)4-Aib-OMe (1: Boc = t-butoxycarbonyl; Aib = alpha-aminoisobutyric acid; DeltaZPhe = Z-alpha,beta-didehydrophenylalanine) to provide the precise conformational parameters of the octapeptide segment -(Aib-DeltaZPhe)4-. Peptide 1 adopted a typical 3(10)-helical conformation characterized by = +/-55.8 degrees (50 degrees -65 degrees), = +/-26.7 degrees (15 degrees -45 degrees), and = +/-179.5 degrees (168 degrees -188 degrees) for the average values of the -(Aib-DeltaZPhe)4- segment (the range of the eight values). The 3(10)-helix contains 3.1 residues per turn, being close to the "perfect 3(10)-helix" characterized by 3.0 residues per turn. NMR and Fourier transform infrared (FTIR) spectroscopy revealed that the 3(10)-helical conformation at the atomic resolution is essentially maintained in solution. Energy minimization of peptide 1 by semiempirical molecular orbital calculation converged to a 3(10)-helical conformation similar to the x-ray crystallographic 3(10)-helix. The preference for a 3(10)-helix in the -(Aib-DeltaZPhe)4- segment is ascribed to strong inducers of the 3(10)-helix inherent in Aib and DeltaZPhe residues-in particular, the Aib residues tend to stabilize a 3(10)-helix more effectively. Therefore, the -(Aib-DeltaZPhe)4- segment is useful to rationally design an optically inactive 3(10)-helical backbone, which will be of great importance to provide novel insights into noncovalent and covalent chiral interactions of a helical peptide with a chiral molecule.

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Photocurrent generation by helical peptide monolayers integrating light harvesting and charge‐transport functions

2013

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In this study, we construct photoenergy-conversion systems with chromophores located with molecular precision to facilitate efficient light harvesting and charge transport. 3(10) -Helical peptides carrying a disulfide group at the N-terminal, linearly arranged six naphthyl groups at the side chains, and an energy acceptor (anthryl, pyrenyl, or N-ethylcarbazolyl group) at the C-terminal were immobilized on a gold surface via a gold-sulfur linkage to form a well-defined self-assembled monolayer with vertical orientation. The monolayer composed of helical peptides terminated with a naphthyl group instead of an energy acceptor was used as control. Upon photoexcitation of the naphthyl groups of the monolayers in solutions containing an electron donor, all the monolayers generated an anodic photocurrent. The photocurrent generation by the monolayers with an acceptor is composed of the following three steps: (1) photon capture by the side-chain naphthyl groups and energy transfer to the terminal acceptor (light harvesting), (2) electron donation from the aqueous donor to the excited acceptor (electron generation), and (3) electron transport from the terminal to gold via the side-chain naphthyl groups (electron hopping). Unfortunately, it was found that introduction of an energy acceptor facilitates the light-harvesting step but suppresses the electron-generation and electron-hopping steps, resulting in slight reduction of the efficiency of photocurrent generation compared to the control system. Further detailed discussion on photoenergy and electron transport processes shows a prospect to realize efficient photocurrent generation systems taking advantages of both light harvesting and charge-transport functions in future.

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Structural and conformational properties of (Z)-?-(1-naphthyl)- dehydroalanine residue

Cited by 17 publications

References 49 publications

A helical arrangement of ?-substituents of dehydropeptides: Synthesis and conformational study of sequential nona- and dodecapeptides possessing (Z)-?-(1-naphthyl)dehydroalanine residues

A helical arrangement of ?-substituents of dehydropeptides: Synthesis and conformational study of sequential nona- and dodecapeptides possessing (Z)-?-(1-naphthyl)dehydroalanine residues

Crystal structure of achiral nonapeptide Boc–(Aib–Δ^zPhe)₄–Aib–OMe at atomic resolution: Evidence for a 3₁₀‐helix

Photocurrent generation by helical peptide monolayers integrating light harvesting and charge‐transport functions

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Structural and conformational properties of (Z)-?-(1-naphthyl)- dehydroalanine residue

Cited by 17 publications

References 49 publications

A helical arrangement of ?-substituents of dehydropeptides: Synthesis and conformational study of sequential nona- and dodecapeptides possessing (Z)-?-(1-naphthyl)dehydroalanine residues

A helical arrangement of ?-substituents of dehydropeptides: Synthesis and conformational study of sequential nona- and dodecapeptides possessing (Z)-?-(1-naphthyl)dehydroalanine residues

Crystal structure of achiral nonapeptide Boc–(Aib–ΔzPhe)4–Aib–OMe at atomic resolution: Evidence for a 310‐helix

Photocurrent generation by helical peptide monolayers integrating light harvesting and charge‐transport functions

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Crystal structure of achiral nonapeptide Boc–(Aib–Δ^zPhe)₄–Aib–OMe at atomic resolution: Evidence for a 3₁₀‐helix