Synthesis and conformation of cyclic hexapeptide cyclo(Pro-Sar-Sar)2

Kimura, Shunsaku; Imanishi, Yukio

doi:10.1016/0141-8130(81)90061-1

Cited by 9 publications

(1 citation statement)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As the hydrophobic helical peptide has 2–3 nm chain length, the sarcosine chain length should be 7–8 nm in the assembly, suggesting a moderately extended conformation of the poly(Sar) chain in the membrane. The 1 H‐NMR spectra of S25D12, S24L14, S22L16 , and S25L20 in methanol showed two kinds of NCH 3 signals due to the coexistence of the cis and trans configurations of sarcosine amides (data not shown), indicating that the poly(Sar) chains are flexible25, 26.…”

Section: Resultsmentioning

confidence: 99%

Rational design of peptide nanotubes for varying diameters and lengths

Ueda

Makino

Imai

et al. 2010

Journal of Peptide Science

View full text Add to dashboard Cite

Amphiphilic helical peptides (Sar)(m) -b-(L-Leu-Aib)(n) (m = 22-25; n = 7, 8, 10) with a hydrophobic block as a right-handed helix were synthesized and their mixtures with (Sar)(25) -b-(D-Leu-Aib)(6) containing the hydrophobic block as a left-handed helix were examined in their molecular assembly formation. The single component (Sar)(25) -b-(D-Leu-Aib)(6) forms peptide nanotubes of 70 nm diameter and 200 nm length. The two-component mixtures of (Sar)(25) -b-(D-Leu-Aib)(6) with (Sar)(24) -b-(L-Leu-Aib)(7) , (Sar)(22) -b-(L-Leu-Aib)(8) , and (Sar)(25) -b-(L-Leu-Aib)(10) yield peptide nanotubes of varying dimensions with 200 nm diameter and 400 nm length, 70 nm diameter and several micrometer length (maximum 30 µm), and 70 nm diameter and 100-600 nm length, respectively. The right-handed and the left-handed helix were thus found to be molecularly mixed due to the stereo-complex formation and to generate nanotubes of different sizes. When the mismatch of the hydrophobic helical length between the two components was of four residues, the longest nanotube was generated. Correspondingly, the hydrophobic helical segments have to interdigitate with an anti-parallel orientation at the hydrophobic core region of the nanotube.

show abstract

Section: Resultsmentioning

confidence: 99%

Rational design of peptide nanotubes for varying diameters and lengths

Ueda

Makino

Imai

et al. 2010

Journal of Peptide Science

View full text Add to dashboard Cite

show abstract

Complex formation with alkali and alkaline earth metal ions of cyclic octapeptides, cyclo(Phe‐Pro)₄, cyclo(Leu‐Pro)₄, and cyclo[Lys(Z)‐Pro]₄

Kimura¹,

Imanishi²

1983

Biopolymers

View full text Add to dashboard Cite

SynopsisComplex formation with alkali and alkaline earth metal ions of cycIic octapeptides, cyclo(Phe-Pro)c, cyclo(Leu-Pro)4, and cyclo[Lys(Z)-Pro]4 was investigated in relation to conformation. In an alcohol solution, cyclo(Phe-Pro)4 did not form complexes. However, cyclo(Leu-Pro)4 and cyclo[Lys(Z)-Pro]4 formed complexes selectively with Ba2+ and Ca2+ ions. Changing the solvent from alcohol to acetonitrile, the complexation behavior was very different. In acetonitrile, c~clo(Phe-Pro)~ was found to form a complex with Ba2+, and CD spectra of cyclo(Leu-Pro)4 and cyclo[Lys(Z)-Pro]4 changed sharply on complexation with K+. Rate constants of the complex formation between the cyclic octapeptides and metal salts were in the range of 0.7-12 L mol-1 min-' in an alcohol solution. One of the two types of complex formation in acetonitrile was much faster than that in an alcohol solution.

show abstract

Ca²⁺ binding cyclic octapeptides having an alternating sar and a hydrophobic amino acid in the sequence

Kimura¹,

Ozeki²,

Imanishi³

1989

Biopolymers

View full text Add to dashboard Cite

Cyclic octapeptides having alternating Sar and hydrophobic amino acid sequences, such as cyclo[Lys(Z)-Sar-Leu-Sar-Leu-Sar-Leu-Sar] (C8KL), cyclo[Glu(OMe)-Sar-Lys(Z)-Sar-Leu-Sar-Leu-Sar] (C8KE, and cyclo[Lys(Suc)-Sar-Leu-Sar-Leu-Sar-Leu-Sar] [C8K(Suc)L, Suc represents succinic acid], were synthesized. These cyclic octapeptides formed a complex selectively with Ca2+. Upon complexation, trans peptide bonds of Sar residues were isomerized to cis peptide bonds. C8KL and C8KE showed very similar characteristics of Ca2+ binding, extraction of Ca2+ from an aqueous solution to a chloroform solution, and Ca2+ transport through a liquid chloroform membrane. C8KL transported Ca2+ across the lipid bilayer membrane above the phase-transition temperature, while C8KE and C8K(Suc)L did not. Therefore, the transport of Ca2+ through the lipid bilayer membrane is very sensitive to the hydrophobicity of the carrier molecule.

show abstract

Synthesis and conformation of cyclic hexapeptide cyclo(Pro-Sar-Sar)2

Cited by 9 publications

References 16 publications

Rational design of peptide nanotubes for varying diameters and lengths

Rational design of peptide nanotubes for varying diameters and lengths

Complex formation with alkali and alkaline earth metal ions of cyclic octapeptides, cyclo(Phe‐Pro)₄, cyclo(Leu‐Pro)₄, and cyclo[Lys(Z)‐Pro]₄

Ca²⁺ binding cyclic octapeptides having an alternating sar and a hydrophobic amino acid in the sequence

Contact Info

Product

Resources

About

Synthesis and conformation of cyclic hexapeptide cyclo(Pro-Sar-Sar)2

Cited by 9 publications

References 16 publications

Rational design of peptide nanotubes for varying diameters and lengths

Rational design of peptide nanotubes for varying diameters and lengths

Complex formation with alkali and alkaline earth metal ions of cyclic octapeptides, cyclo(Phe‐Pro)4, cyclo(Leu‐Pro)4, and cyclo[Lys(Z)‐Pro]4

Ca2+ binding cyclic octapeptides having an alternating sar and a hydrophobic amino acid in the sequence

Contact Info

Product

Resources

About

Complex formation with alkali and alkaline earth metal ions of cyclic octapeptides, cyclo(Phe‐Pro)₄, cyclo(Leu‐Pro)₄, and cyclo[Lys(Z)‐Pro]₄

Ca²⁺ binding cyclic octapeptides having an alternating sar and a hydrophobic amino acid in the sequence