Folding pentapeptides into left and right handed alpha helices
Identifieur interne : 004D16 ( PascalFrancis/Curation ); précédent : 004D15; suivant : 004D17Folding pentapeptides into left and right handed alpha helices
Auteurs : Huy N. Hoang [Australie] ; Giovanni Abbenante [Australie] ; Timothy A. Hill [Australie] ; Gloria Ruiz-Gomez [Australie] ; David P. Fairlie [Australie]Source :
- Tetrahedron : (Oxford. Print) [ 0040-4020 ] ; 2012.
Descripteurs français
- Pascal (Inist)
- Wicri :
English descriptors
- KwdEn :
Abstract
Left or right handed alpha helicity can be induced in a pentapeptide (ANGYG) by appending left or right handed helical cycles as chiral templates. This sequence corresponds to a rare left handed helix found in the protein alanine racemase. Circular dichroism spectra reveal that pentapeptide ANGYG has no detectable structure in aq phosphate buffer, that it is an ambidextrous peptide in that it can be directed to fold into either a left handed or right handed alpha helix in water, with greater propensity for the uncommon left handed than the normal right handed conformation. A helix-inducing cyclic peptide at both ends of this peptide was more effective at inducing alpha helicity than a single cyclic peptide at one end. The alpha helical cyclic peptides provide novel tools for folding short peptides into thermodynamically unstable helices in water, and for studying factors that control chirality and helix induction.
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<author><name sortKey="Hill, Timothy A" sort="Hill, Timothy A" uniqKey="Hill T" first="Timothy A." last="Hill">Timothy A. Hill</name>
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<author><name sortKey="Ruiz Gomez, Gloria" sort="Ruiz Gomez, Gloria" uniqKey="Ruiz Gomez G" first="Gloria" last="Ruiz-Gomez">Gloria Ruiz-Gomez</name>
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<term>Buffer system</term>
<term>Chiral compound</term>
<term>Chirality</term>
<term>Circular dichroism</term>
<term>Circular dichroism spectrometry</term>
<term>Conformation</term>
<term>Cyclic peptides</term>
<term>Folding</term>
<term>Helical structure</term>
<term>Helicity</term>
<term>Molecular structure</term>
<term>Pentapeptide</term>
<term>Phosphates</term>
<term>Phosphorus Organic compounds</term>
<term>Protein</term>
<term>Water</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Pliage</term>
<term>Pentapeptide</term>
<term>Structure hélice</term>
<term>Hélicité</term>
<term>Composé chiral</term>
<term>Protéine</term>
<term>Alanine racemase</term>
<term>Spectrométrie CD</term>
<term>Structure moléculaire</term>
<term>Système tampon</term>
<term>Peptide cyclique</term>
<term>Eau</term>
<term>Conformation</term>
<term>Chiralité</term>
<term>Dichroïsme circulaire</term>
<term>Phosphate</term>
<term>Phosphore Composé organique</term>
<term>Foldamère</term>
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<front><div type="abstract" xml:lang="en">Left or right handed alpha helicity can be induced in a pentapeptide (ANGYG) by appending left or right handed helical cycles as chiral templates. This sequence corresponds to a rare left handed helix found in the protein alanine racemase. Circular dichroism spectra reveal that pentapeptide ANGYG has no detectable structure in aq phosphate buffer, that it is an ambidextrous peptide in that it can be directed to fold into either a left handed or right handed alpha helix in water, with greater propensity for the uncommon left handed than the normal right handed conformation. A helix-inducing cyclic peptide at both ends of this peptide was more effective at inducing alpha helicity than a single cyclic peptide at one end. The alpha helical cyclic peptides provide novel tools for folding short peptides into thermodynamically unstable helices in water, and for studying factors that control chirality and helix induction.</div>
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<fC01 i1="01" l="ENG"><s0>Left or right handed alpha helicity can be induced in a pentapeptide (ANGYG) by appending left or right handed helical cycles as chiral templates. This sequence corresponds to a rare left handed helix found in the protein alanine racemase. Circular dichroism spectra reveal that pentapeptide ANGYG has no detectable structure in aq phosphate buffer, that it is an ambidextrous peptide in that it can be directed to fold into either a left handed or right handed alpha helix in water, with greater propensity for the uncommon left handed than the normal right handed conformation. A helix-inducing cyclic peptide at both ends of this peptide was more effective at inducing alpha helicity than a single cyclic peptide at one end. The alpha helical cyclic peptides provide novel tools for folding short peptides into thermodynamically unstable helices in water, and for studying factors that control chirality and helix induction.</s0>
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<fC02 i1="03" i2="X"><s0>001C03C01A</s0>
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<fC03 i1="01" i2="X" l="FRE"><s0>Pliage</s0>
<s5>01</s5>
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<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Doblado</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Pentapeptide</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Pentapeptide</s0>
<s5>02</s5>
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<fC03 i1="02" i2="X" l="SPA"><s0>Pentapéptido</s0>
<s5>02</s5>
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<fC03 i1="03" i2="X" l="FRE"><s0>Structure hélice</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Helical structure</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Estructura helicoidal</s0>
<s5>03</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Hélicité</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Helicity</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Helicidad</s0>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Composé chiral</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Chiral compound</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Compuesto quiral</s0>
<s5>05</s5>
</fC03>
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<s5>06</s5>
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<s5>06</s5>
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<fC03 i1="07" i2="X" l="FRE"><s0>Alanine racemase</s0>
<s2>FE</s2>
<s5>07</s5>
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<fC03 i1="07" i2="X" l="ENG"><s0>Alanine racemase</s0>
<s2>FE</s2>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Alanine racemase</s0>
<s2>FE</s2>
<s5>07</s5>
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<fC03 i1="08" i2="X" l="FRE"><s0>Spectrométrie CD</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Circular dichroism spectrometry</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Espectrometría CD</s0>
<s5>08</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>Structure moléculaire</s0>
<s5>09</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Molecular structure</s0>
<s5>09</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>Estructura molecular</s0>
<s5>09</s5>
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<fC03 i1="10" i2="X" l="FRE"><s0>Système tampon</s0>
<s5>11</s5>
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<s5>11</s5>
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<s5>11</s5>
</fC03>
<fC03 i1="11" i2="X" l="FRE"><s0>Peptide cyclique</s0>
<s5>12</s5>
</fC03>
<fC03 i1="11" i2="X" l="ENG"><s0>Cyclic peptides</s0>
<s5>12</s5>
</fC03>
<fC03 i1="11" i2="X" l="SPA"><s0>Péptido cíclico</s0>
<s5>12</s5>
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<fC03 i1="12" i2="X" l="FRE"><s0>Eau</s0>
<s5>13</s5>
</fC03>
<fC03 i1="12" i2="X" l="ENG"><s0>Water</s0>
<s5>13</s5>
</fC03>
<fC03 i1="12" i2="X" l="SPA"><s0>Agua</s0>
<s5>13</s5>
</fC03>
<fC03 i1="13" i2="X" l="FRE"><s0>Conformation</s0>
<s5>14</s5>
</fC03>
<fC03 i1="13" i2="X" l="ENG"><s0>Conformation</s0>
<s5>14</s5>
</fC03>
<fC03 i1="13" i2="X" l="SPA"><s0>Conformación</s0>
<s5>14</s5>
</fC03>
<fC03 i1="14" i2="X" l="FRE"><s0>Chiralité</s0>
<s5>15</s5>
</fC03>
<fC03 i1="14" i2="X" l="ENG"><s0>Chirality</s0>
<s5>15</s5>
</fC03>
<fC03 i1="14" i2="X" l="SPA"><s0>Quiralidad</s0>
<s5>15</s5>
</fC03>
<fC03 i1="15" i2="X" l="FRE"><s0>Dichroïsme circulaire</s0>
<s5>16</s5>
</fC03>
<fC03 i1="15" i2="X" l="ENG"><s0>Circular dichroism</s0>
<s5>16</s5>
</fC03>
<fC03 i1="15" i2="X" l="SPA"><s0>Dicroismo circular</s0>
<s5>16</s5>
</fC03>
<fC03 i1="16" i2="X" l="FRE"><s0>Phosphate</s0>
<s2>NA</s2>
<s5>17</s5>
</fC03>
<fC03 i1="16" i2="X" l="ENG"><s0>Phosphates</s0>
<s2>NA</s2>
<s5>17</s5>
</fC03>
<fC03 i1="16" i2="X" l="SPA"><s0>Fosfato</s0>
<s2>NA</s2>
<s5>17</s5>
</fC03>
<fC03 i1="17" i2="X" l="FRE"><s0>Phosphore Composé organique</s0>
<s2>NC</s2>
<s2>NA</s2>
<s5>41</s5>
</fC03>
<fC03 i1="17" i2="X" l="ENG"><s0>Phosphorus Organic compounds</s0>
<s2>NC</s2>
<s2>NA</s2>
<s5>41</s5>
</fC03>
<fC03 i1="17" i2="X" l="SPA"><s0>Fósforo Compuesto orgánico</s0>
<s2>NC</s2>
<s2>NA</s2>
<s5>41</s5>
</fC03>
<fC03 i1="18" i2="X" l="FRE"><s0>Foldamère</s0>
<s4>INC</s4>
<s5>62</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Isomerases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Isomerases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Isomerases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
</fC07>
<fN21><s1>247</s1>
</fN21>
</pA>
</standard>
</inist>
</record>
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