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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-1-25
pubmed:abstractText
A model for the nucleation of crystallization in peptide helices is presented. The crystal structures of four polymorphic forms of a hydrophobic helical decapeptide Boc-Leu-Aib-Phe-Phe-Leu-Aib-Ala-Ala-Leu-Aib-OMe (I) exemplify alternative packing modes in cylindrical molecules. Three crystal forms of peptide I are monoclinic P2(1), while one is orthorhombic P22121. The five different helical molecules characterized have very similar backbone conformations over much of the peptide length. A survey of 117 helical peptide structures with a length >/=8 residues reveals a preponderance of the triclinic (P1), monoclinic (P2(1)), and orthorhombic (P2(1)2(1)2(1)) crystal forms. Models for the formation of critical nuclei are based on helix association driven by solvophobic forces, resulting in the formation of raftlike structures. Raft association can be further driven by the imperative of minimizing solvent accessible surface area with the formation of blocks, which can be subsequently fitted in Lego set fashion by multiple hydrogen bond interactions in the head-to-tail region. This model provides a rationalization for observed crystal formation based on a postulated structure for an embryonic nucleus, which is determined by aggregation patterns and unconstrained by the dictates of symmetry.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1520-6106
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
112
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1308-14
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Nucleation, growth, and form in crystals of peptide helices.
pubmed:affiliation
Department of Physics, Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't