Expected and unexpected effects of amino acid substitutions on polypeptide-directed crystal growth

Katya Delak, Sebastiano Collino, John Evans

Research output: Contribution to journalArticle

Abstract

Nature's use of biomineralization polypeptides to control and modulate the growth of biogenic minerals is an important process that, if properly understood, could have significant implications for designing and creating new inorganic-based materials. Although the sequences for a number of biomineralization proteins exist, very little is known about the participation of specific amino acids in the mineral modulation process. In this letter, we investigate the impact of global Asp → Asn and Glu → Gln substitutions on two mollusk shell nacre polypeptides, AP7N and n16N. We find that these global substitutions, which remove all anionic Ca(II) binding sites, abolish the expected in vitro mineralization activities associated with each native polypeptide. In addition, the ability of substituted peptides to form complexes with both Ca(II) and Ca(II) metal ion analogs is also abolished. However, some unexpected effects were noted. First, the Asp → Asn, Glu → Gln substituted n16N polypeptide is observed to self-assemble and form biofilms or coatings that appear to mineralize in vitro. Second, both polypeptides are structurally affected by these substitutions, with Asp → Asn substituted AP7N transforming to an a helix and Asp → Asn, Glu → Gln substituted n16N transforming to a more unfolded random-coil-like structure. We find that the participation of Asp and Glu residues is crucial to the inherent mineralization activities and conformations of AP7N and n16N polypeptides. Surprisingly, we find that the replacement of anionic residues within biomineralization polypeptides such as n16N still permits mineral modulation, but in a different form that now involves peptide self-association and biofilm formation.

Original languageEnglish (US)
Pages (from-to)11951-11955
Number of pages5
JournalLangmuir
Volume23
Issue number24
DOIs
StatePublished - Nov 20 2007

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Polypeptides
polypeptides
Crystallization
Crystal growth
amino acids
Amino acids
crystal growth
Substitution reactions
substitutes
Amino Acids
Peptides
Biomineralization
biofilms
Minerals
minerals
Biofilms
peptides
mollusks
Modulation
modulation

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

Expected and unexpected effects of amino acid substitutions on polypeptide-directed crystal growth. / Delak, Katya; Collino, Sebastiano; Evans, John.

In: Langmuir, Vol. 23, No. 24, 20.11.2007, p. 11951-11955.

Research output: Contribution to journalArticle

Delak, Katya ; Collino, Sebastiano ; Evans, John. / Expected and unexpected effects of amino acid substitutions on polypeptide-directed crystal growth. In: Langmuir. 2007 ; Vol. 23, No. 24. pp. 11951-11955.
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