Design of α-helical peptides: Their role in protein folding and molecular biology

Parthasarathy, R.; Chaturvedi, Sanjeev; Go, K.

doi:10.1016/0079-6107(95)00009-7

Cited by 31 publications

(24 citation statements)

References 164 publications

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“…Therefore, it is presumed that amino acid sequences with negative charges at the N-terminus and positive charges at the C-terminus can enhance and stabilize the helical dipole moment, and in turn the helix itself. This phenomenon has been found to be statistically significant, and many helices in proteins agree with this predictioñ Hol, 1985;Parthasarathy et al, 1995!. It should be emphasized that not all helices have such a charge arrangement.…”

Section: Implications For Inhibitors Of Amyloid Formationsupporting

confidence: 51%

“…Other aspects of structural plasticity a-Helices have a helical dipole moment along the backbone that possesses a directionality from C r N. Many a-helices have a preference for negatively charged residues located at the N-terminus and positively charged residues located at the C-terminus called helix capping~Blagdon & Goodman, 1975;Hol, 1985;Presta & Rose, 1988;Parthasarathy et al, 1995;Aurora & Rose, 1998!. It has been postulated that the a-helix may be considered as an array of dipoles arranged in such a way in that they orient along the axis of the helix with the negative pole at the C-terminus and the positive pole at the N-terminus~Blagdon & Goodman, 1975!.…”

Section: Implications For Inhibitors Of Amyloid Formationmentioning

confidence: 99%

“…This property is perhaps related to their primary sequence. They contain hydrophobic faces that are important to the formation of b-sheet assemblies Rippon et al, 1973;Brack & Orgel, 1975;Osterman & Kaiser, 1981;Zhang et al, 1993;Xiong et al, 1995;Zhang & Rich, 1997;West et al, 1999!, as well as a dipole charge distribution and helix capping consistent with a-helical stability~Blagdon & Goodman, 1975;Hol et al, 1981;Hol, 1985;Presta & Rose, 1988;Harper & Rose, 1993;Huyghues-Despointes et al, 1993;Parthasarathy et al, 1995;Aurora & Rose, 1998!. It has also been reported that sequence dependence of secondary structure formation in host-guest peptides with either a-helix or b-sheet structure can be influenced by the supporting media~Mutter et al, 1985!.…”

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confidence: 99%

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Conformational behavior of ionic self‐complementary peptides

et al. 2000

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Several de novo designed ionic peptides that are able to undergo conformational change under the influence of temperature and pH were studied. These peptides have two distinct surfaces with regular repeats of alternating hydrophilic and hydrophobic side chains. This permits extensive ionic and hydrophobic interactions resulting in the formation of stable b-sheet assemblies. The other defining characteristic of this type of peptide is a cluster of negatively charged aspartic or glutamic acid residues located toward the N-terminus and positively charged arginine or lysine residues located toward the C-terminus. This arrangement of charge balances the a-helical dipole moment~C r N!, resulting in a strong tendency to form stable a-helices as well. Therefore, these peptides can form both stable a-helices and b-sheets. They are also able to undergo abrupt structural transformations between these structures induced by temperature and pH changes. The amino acid sequence of these peptides permits both stable b-sheet and a-helix formation, resulting in a balance between these two forms as governed by the environment. Some segments in proteins may also undergo conformational changes in response to environmental changes. Analyzing the plasticity and dynamics of this type of peptide may provide insight into amyloid formation. Since these peptides have dynamic secondary structure, they will serve to refine our general understanding of protein structure.

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Section: Implications For Inhibitors Of Amyloid Formationsupporting

confidence: 51%

Section: Implications For Inhibitors Of Amyloid Formationmentioning

confidence: 99%

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confidence: 99%

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Conformational behavior of ionic self‐complementary peptides

et al. 2000

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“…[2,3] Many strategies have been pursued to design peptide helices [4][5][6][7] and notable results have been achieved even with very short sequences, [8] but mainly these methods rely on the use of nonnatural amino acids or introducing constraints. [8][9][10][11][12][13] In this paper, we report on the stability characterization, using CD, NMR and MD studies, of a designed, a-helical, 15-mer peptide (named QK), composed only of natural amino acids (sequence Ac-KLTWQELYQLKYKGI-NH 2 ), which activates the VEGFdependent angiogenic response.…”

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confidence: 99%

Structural Determinants of the Unusual Helix Stability of a De Novo Engineered Vascular Endothelial Growth Factor (VEGF) Mimicking Peptide

Diana¹,

Ziaco

Colombo

et al. 2008

Chemistry A European J

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Helix stability: Understanding helix stability and formation is a prerequisite to elucidate the mechanism of protein folding and design helix peptides with specific activity. Herein, we analyze the thermal behaviour of a designed, α-helical, bioactive peptide, composed only of natural amino acids. This peptide shows an unusual thermal stability, in which the N-terminal region and a hydrophobic interaction play a major role

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“…As a potential advantage, such sterically constrained peptoid side chains could be entropically favorable leading to improved binding affinity. Alternatively, the occasional unusual conformations adopted by proline [32], its significant flexibility which generates a kink along the α-helix [33]–[35], or rapid cis / trans isomerization [36] can have negative consequences for binding affinity. It is postulated that perturbation of structural features of the α-helix in these proline-substituted C 20 peptide predominates, thereby interfering in binding of the proline-substituted C 20 peptides to the target.…”

Section: Resultsmentioning

confidence: 99%

A Readily Applicable Strategy to Convert Peptides to Peptoid-based Therapeutics

et al. 2013

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Incorporation of unnatural amino acids and peptidomimetic residues into therapeutic peptides is highly efficacious and commonly employed, but generally requires laborious trial-and-error approaches. Previously, we demonstrated that C20 peptide has the potential to be a potential antiviral agent. Herein we report our attempt to improve the biological properties of this peptide by introducing peptidomimetics. Through combined alanine, proline, and sarcosine scans coupled with a competitive fluorescence polarization assay developed for identifying antiviral peptides, we enabled to pinpoint peptoid-tolerant peptide residues within C20 peptide. The synergistic benefits of combining these (and other) commonly employed methods could lead to a easily applicable strategy for designing and refining therapeutically-attractive peptidomimetics.

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Design of α-helical peptides: Their role in protein folding and molecular biology

Cited by 31 publications

References 164 publications

Conformational behavior of ionic self‐complementary peptides

Conformational behavior of ionic self‐complementary peptides

Structural Determinants of the Unusual Helix Stability of a De Novo Engineered Vascular Endothelial Growth Factor (VEGF) Mimicking Peptide

A Readily Applicable Strategy to Convert Peptides to Peptoid-based Therapeutics

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