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. 2010 Jan 1;86(1):111-130.
doi: 10.1080/00218460903418154.

Structural and Biophysical Characterization of a Cyclic Bioadhesive With Cell Attachment Ability

Marion P Olivieri  1 , Robert M Wollman  2 , Mary I Hurley  1 , Michael F Swartz  3
Affiliations

Structural and Biophysical Characterization of a Cyclic Bioadhesive With Cell Attachment Ability

Marion P Olivieri et al. J Adhes. .

Abstract

Structural and cellular attachment analysis identified overall bent helical regions of adhesive peptides identified within mussel adhesive protein (MAP) capable of also attaching cells. DOPA (L-DOPA, 3,4-dihydroxyphenylalanine) is frequently identified and credited for the attachment ability of several marine proteins [Olivieri, MP, et al. (2002), Biofouling18, 149-159]. Newly designed cyclic peptides (DOPA-G-G-C-G-K-A-K-G-C [cyc-DOPA] & Y-G-G-C-G-K-A-K-G-C [cyc-Y]) derived from structurally conserved regions of several MAP peptides were examined to assist in the understanding of both surface and cellular attachment. Solution-state proton nuclear magnetic resonance (NMR) spectroscopy coupled with molecular modeling and dynamics revealed minimal differences in the structures of the proposed cellular attachment domain within these two peptides. Multiple attenuated internal reflection infrared (MAIR-IR) spectroscopy, ellipsometry and advancing contact angle analyses showed that formation of thin films by these peptides was L-DOPA and pH dependent. When compared to control surfaces, undifferentiated leukocyte cells (MOLT-4) significantly attached and spread onto films created from the cyc-DOPA. The culmination of these structural, biophysical and cellular attachment techniques reveal a conformation of cyc-DOPA that is capable of both adsorbing to surfaces and then attaching cells that spread. This work supports the sequence, K-A-K, as the cellular attachment domain, especially when held in a reliable structural conformation.,.

Keywords: NMR; cell attachment; peptide structure; protein adsorption; surface chemistry.

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Figures

Figure 1
Figure 1
MAIR-IR spectrum of a cyc-DOPA film created from 2μg/cm2 after rinsing.
Figure 2
Figure 2
Number of MOLT-4 leukocytes attached over a total 8 cm2 region in the absence (top) and presence of albumin introduction (bottom). Going from left to right conditions included cyc-DOPA, MAP-RD, cyc-Y, TCPS, and MAP.
Figure 3
Figure 3
SEM image of a MOLT-4 cell attached and spread onto a cyc-DOPA film.
Figure 4
Figure 4
Fingerprint region of a ROESY spectrum of cyc-DOPA at 600 MHz with a mixing time of 300ms.
Figure 5
Figure 5
Family of the 10 lowest energy structures resulting from nOe data, distance geometry calculations (DIANA) and molecular modeling of cyc-DOPA.
Figure 6
Figure 6
RMSD per residue of the family of ten cyc-DOPA structures after simulated annealing. White is Cα-C-N, grey is Cα-C-O-N, black is all heavy atoms.
Figure 7
Figure 7
RMSD for each dynamic time point to the mean dynamic structure for the backbone (black) and for all heavy atoms (grey) over the time course of a 200 ps dynamics experiment.
Figure 8
Figure 8
The dynamics averaged structures of cyc-DOPA (left) and cyc-Y (right).
See this image and copyright information in PMC

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References

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