Circular dichroism studies of an elastin crosslinked peptide

Circular dichroic studies of a desmosine crosslinked peptide reveal a hitherto undescribed elastin spectrum possessing a weak negative band at 230–235 nm, a weak positive band at 215 nm, and a maximum negative band at 190 nm. The spectrum is sensitive to both pH and temperature displaying increased ellipticity of the 215‐nm band at acidic pH and low temperature. The general shape of the spectrum and its behaviour toward temperature changes suggest the presence of an extended helical conformation. Susceptibility of insoluble elastin to digestion with chymotrypsin is increased tenfold at low temperature (4°C), supporting the contention that the conformational change of the type described above occurs in insoluble elastin. Such changes in conformation would result in increased availability of aromatic amino‐acid resiudues to peptide bond cleavage.

[1]  A. Glazer,et al.  An analysis of the tyrosine circular dichroism bands in ribonuclease. , 1967, Journal of the American Chemical Society.

[2]  A. Walton,et al.  Synthesis and characterization of poly(LysAla3) , 1974, Biopolymers.

[3]  S. Krimm,et al.  Circular dichroism of the “random” polypeptide chain , 1969 .

[4]  Soluble fragments of elastin. Circular dichroism studies. , 2009, International journal of peptide and protein research.

[5]  W R Gray,et al.  Isolation and amino acid sequences of tropoelastin peptides. , 1973, The Journal of biological chemistry.

[6]  D. W. Smith,et al.  The purification and partial characterization of a soluble elastin-like protein from copper-deficient porcine aorta. , 1969, Biochemistry.

[7]  H. Kagan,et al.  Proteolysis of elastin-ligand complexes. Stimulation of elastase digestion of insoluble elastin by sodium dodecyl sulfate. , 1972, Biochemistry.

[8]  A. Walton,et al.  Characterization of two sequential polytripeptides containing glycine and ethyl‐glutamate residues , 1972, Biopolymers.

[9]  M. Levi,et al.  Antigenicity and chemical composition of an enzymatic digest of elastin. , 1969, Archives of biochemistry and biophysics.

[10]  D. Urry,et al.  Coacervation and ion-binding studies on aortic elastin. , 1973, Biochimica et biophysica acta.

[11]  L. Sandberg,et al.  Molecular Model for Elastin Structure and Function , 1973, Nature.

[12]  L B Sandberg,et al.  Isolation and characterization of cross-linked peptides from elastin. , 1974, The Journal of biological chemistry.

[13]  G. Stark.  [7] Use of cyanate for determining NH(2)-terminal residues in protein. , 1972, Methods in enzymology.

[14]  S. M. Partridge,et al.  The chemistry of connective tissues. 3. Composition of the soluble proteins derived from elastin. , 1955, The Biochemical journal.

[15]  A. Berger,et al.  Synthesis and conformation of poly(L‐lysyl‐L‐alanyl), a sequence‐ordered water‐soluble copolymer , 1972, Biopolymers.

[16]  L. Sandberg,et al.  Structural features of tropoelastin related to the sites of cross-links in aortic elastin. , 1971, Biochemistry.

[17]  B. Sykes,et al.  Salt-soluble elastin from lathyritic chicks. , 1974, The Biochemical journal.

[18]  D. Smyth.  [24] Techniques in enzymic hydrolysis , 1967 .

[19]  T. J. Bronzert,et al.  Analysis of amino acid phenylthiohydantoins by gas chromatography. , 1969, The Journal of biological chemistry.

[20]  J. E. Mark,et al.  Conformations of polypeptides with ionized side chains of equal length. , 1968, Proceedings of the National Academy of Sciences of the United States of America.

[21]  J. Jones,et al.  A synthetic polypeptide related to elastin and its interaction with calcium ions. , 2009, International journal of peptide and protein research.

[22]  L. Sandberg,et al.  A new method for purification of mature elastin. , 1975, Analytical biochemistry.