Bovine Elastin and κ-Elastin Secondary Structure Determination by Optical Spectroscopies (*)

Elastin is the macromolecular polymer of tropoelastin molecules responsible for the elastic properties of tissues. The understanding of its specific elasticity is uncertain because its structure is still unknown. Here, we report the first experimental quantitative determination of bovine elastin secondary structures as well as those of its corresponding soluble κ-elastin. Using circular dichroism and Fourier transform infrared and near infrared Fourier transform Raman spectroscopic data, we estimated the secondary structure contents of elastin to be ∼10% α-helices, ∼45% β-sheets, and ∼45% undefined conformations. These values were very close to those we had previously determined for the free monomeric tropoelastin molecule, suggesting thus that elastin would be constituted of a closely packed assembly of globular β structural class tropoelastin molecules cross-linked to form the elastic network (liquid drop model of elastin architecture). The presence of a strong hydration shell is demonstrated for elastin, and its possible contribution to elasticity is discussed.

[1]  W. T. Grandy.  Maximum entropy in action: Buck, Brian and Macaulay, Vincent A., 1991, 220 pp., Clarendon Press, Oxford, £30 pb, ISBN 0-19-8539630 , 1995 .

[2]  K. Raju,et al.  Primary structures of bovine elastin a, b, and c deduced from the sequences of cDNA clones. , 1987, The Journal of biological chemistry.

[3]  R. Mecham,et al.  The cysteine residues in the carboxy terminal domain of tropoelastin form an intrachain disulfide bond that stabilizes a loop structure and positively charged pocket. , 1992, Biochemical and biophysical research communications.

[4]  Alain J. P. Alix,et al.  Determination of the secondary structure of proteins from the Raman amide I band: the reference intensity profiles method , 1987 .

[5]  F. Parker.  Applications of Infrared, Raman, and Resonance Raman Spectroscopy in Biochemistry , 1983 .

[6]  Joseph L. Walter,et al.  The Infrared Spectra of Complex Molecules , 1982 .

[7]  Alain J. P. Alix,et al.  Optical spectroscopic determination of bovine tropoelastin molecular model , 1995 .

[8]  Dan W. Urry,et al.  Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics , 1988, Journal of protein chemistry.

[9]  L Peltonen,et al.  Alternative splicing of human elastin mRNA indicated by sequence analysis of cloned genomic and complementary DNA. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[10]  G. Abatangelo,et al.  Conformational transitions of alpha-elastin. , 1977, Biochimica et biophysica acta.

[11]  W. Caughey,et al.  Protein secondary structures in water from second-derivative amide I infrared spectra. , 1990, Biochemistry.

[12]  J. R. Lyerla,et al.  Molecular mobility and structure of elastin deduced from the solvent and temperature dependence of 13C magnetic resonance relaxation data. , 1975, Biochemistry.

[13]  R. Mecham,et al.  The Elastic Fiber , 1991 .

[14]  MJ Miles,et al.  Protein Assemblies and Single Molecules Imaged by STM , 1993 .

[15]  P J Flory,et al.  The elastic properties of elastin , 1974, Biopolymers.

[16]  J. Koenig,et al.  Raman scattering of collagen, gelatin, and elastin , 1975, Biopolymers.

[17]  R. Mecham,et al.  Microfibril-associated glycoprotein binds to the carboxyl-terminal domain of tropoelastin and is a substrate for transglutaminase. , 1994, The Journal of biological chemistry.

[18]  J. Huvenne,et al.  Spectroscopy of Biological Molecules , 1995, Springer Netherlands.

[19]  Michel Manfait,et al.  Spectroscopy of Biological Molecules , 1985 .

[20]  J. Gosline,et al.  The effects of polar solutes on the viscoelastic behavior of elastin. , 1993, Biorheology.

[21]  J. Bandekar,et al.  Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. , 1986, Advances in protein chemistry.

[22]  S. O. Andersen,et al.  New Molecular Model for the Long-range Elasticity of Elastin , 1970, Nature.

[23]  J L Lippert,et al.  Laser Raman studies of conformational variations of poly‐L‐lysine , 1973, Biopolymers.

[24]  D. Torchia,et al.  Characterization of molecular motions in 13C‐labeled aortic elastin by 13C‐1H magnetic double resonance , 1980, Biopolymers.

[25]  M. Spina,et al.  Application of affinity chromatography to the purification of collagenase for the isolation of insoluble elastin. , 1975, Biochimica et biophysica acta.

[26]  C. Lacabanne,et al.  Solid-state studies on synthetic fragments and analogues of elastin. , 1993, International journal of biological macromolecules.

[27]  D. Urry,et al.  What is elastin; what is not. , 1983, Ultrastructural pathology.

[28]  Conformational analysis by molecular mechanics energy minimizations of the tetrapeptide Boc-Gly-Leu-Gly-Gly–NMe, a recurring sequence of elastin , 1993 .

[29]  Z. Indik,et al.  Sequence variation of bovine elastin mRNA due to alternative splicing. , 1987, Collagen and related research.

[30]  S. Provencher,et al.  Estimation of globular protein secondary structure from circular dichroism. , 1981, Biochemistry.

[31]  B. Malcolm.  Peptides, polypeptides and proteins , 1976 .

[32]  A. Tamburro,et al.  Molecular mechanics calculations of the conformers of the dipetide Boc–Gly–Leu–NMe and tripeptide Boc–Gly–Leu–Gly–NMe. Searching the conformational space by the build-up method , 1992 .

[33]  L. J. Bellamy.  The infra-red spectra of complex molecules , 1962 .

[34]  L. J. Bellamy.  The infra-red spectra of complex molecules , 1962 .

[35]  G. Abatangelo,et al.  Concentration-dependent conformational transition of alpha-elastin in aqueous solution. , 1978, The Journal of biological chemistry.

[36]  R. Williams.  Protein secondary structure analysis using Raman amide I and amide III spectra. , 1986, Methods in enzymology.

[37]  Anthony T. Tu,et al.  Raman spectroscopy in biology: Principles and applications , 1982 .

[38]  H. Mantsch,et al.  Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. , 1993, Biochemistry.

[39]  J. Gosline,et al.  The effects of hydration on the dynamic mechanical properties of elastin , 1990, Biopolymers.

[40]  C. Lacabanne,et al.  Phase transitions and chain dynamics, in the solid state, of a pentapeptide sequence of elastins. , 1992, International journal of biological macromolecules.

[41]  G. Pezzin,et al.  Evidence for Order in the Structure of α-Elastin , 1968, Nature.

[42]  G. J. Thomas,et al.  Appendix: Raman spectrum and structure of elastin in relation to type‐II β‐turns , 1987 .

[43]  F. Goñi,et al.  Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. , 1993, Progress in biophysics and molecular biology.

[44]  Douglas J. Moffatt,et al.  Fourier Self-Deconvolution: A Method for Resolving Intrinsically Overlapped Bands , 1981 .

[45]  A. Tamburro,et al.  Synthesis and structural studies of a pentapeptide sequence of elastin. Poly (Val-Gly-Gly-Leu-Gly). , 1992, Journal of biomolecular structure & dynamics.

[46]  W. C. Johnson,et al.  Sensitivity of circular dichroism to protein tertiary structure class , 1983, Nature.