Online citations, reference lists, and bibliographies.
Please confirm you are human
(Sign Up for free to never see this)
← Back to Search

Recombinant Mussel Protein Pvfp-5β: A Potential Tissue Bioadhesive

Radha Santonocito, Francesca Venturella, F. Dal Piaz, M. A. Morando, A. Provenzano, E. Rao, M. A. Costa, Donatella Bulone, P. L. San Biagio, D. Giacomazza, Alessandro Sicorello, Caterina Alfano, Rosa Passantino, A. Pastore
Published 2019 · Chemistry, Medicine

Save to my Library
Download PDF
Analyze on Scholarcy
Share
During their lifecycle, many marine organisms rely on natural adhesives to attach to wet surfaces for movement and self-defense in aqueous tidal environments. Adhesive proteins from mussels are biocompatible and elicit only minimal immune responses in humans. Therefore these proteins have received increased attention for their potential applications in medicine, biomaterials, and biotechnology. The Asian green mussel Perna viridis secretes several byssal plaque proteins, molecules that help anchoring the mussel to surfaces. Among these proteins, protein-5β (Pvfp-5β) initiates interactions with the substrate, displacing interfacial water molecules before binding to the surface. Here, we established the first recombinant expression in Escherichia coli of Pvfp-5β. We characterized recombinant Pvfp-5β, finding that despite displaying a CD spectrum consistent with features of a random coil, the protein is correctly folded as indicated by MS and NMR analyses. Pvfp-5β folds as a β-sheet–rich protein as expected for an epidermal growth factor-like module. We examined the effects of Pvfp-5β on cell viability and adhesion capacity in NIH-3T3 and HeLa cell lines, revealing that Pvfp-5β has no cytotoxic effects at the protein concentrations used and provides good cell-adhesion strength on both glass and plastic plates. Our findings suggest that the adhesive properties of recombinant Pvfp-5β make it an efficient surface-coating material, potentially suitable for biomedical applications including regeneration of damaged tissues.
This paper references
10.1021/acs.biochem.5b01177
α,β-Dehydro-Dopa: A Hidden Participant in Mussel Adhesion.
R. Mirshafian (2016)
10.1021/bm301908y
Adhesion of mussel foot protein-3 to TiO2 surfaces: the effect of pH.
J. Yu (2013)
The use of adhesives in chondro - cyte transplantation surgery : preliminary studies : bulletin of the Hospital for Joint Diseases Orthopaedic Institute
D. A. Grande (1988)
10.1002/biot.200700258
Development of bioadhesives from marine mussels
H. J. Cha (2008)
A glyco- sylated byssal precursor protein from the green mussel Perna viridis with modified dopa
K. Ohkawa (2004)
10.1039/C2SM25173F
Adhesion mechanism in a DOPA-deficient foot protein from green mussels().
D. Hwang (2012)
10.1016/j.actbio.2018.04.034
Bioadhesives for internal medical applications: A review.
Wenzhen Zhu (2018)
Accelerating the design of biomi- metic materials by integrating RNA-seq with proteomics and materials science
P. A. Guerette (2013)
10.1080/08927010410001681246
A Glycosylated Byssal Precursor Protein from the Green Mussel Perna viridis with Modified Dopa Side-chains
Kousaku Ohkawa (2004)
10.1080/08927014.2015.1026337
Interfacial pH during mussel adhesive plaque formation
Nadine R. Martinez Rodriguez (2015)
10.1074/jbc.M110.133157
Protein- and Metal-dependent Interactions of a Prominent Protein in Mussel Adhesive Plaques*
D. Hwang (2010)
5-(3-carboxymethoxyphenyl)- 2(4,5-dimethylthiazolyl)-3-(4-sulfophenyl)tetrazolium, inner salt (MTS) and related at K
John A. Barltrop (2019)
10.14219/JADA.ARCHIVE.1986.0116
Adhesive protein from mussels: possibilities for dentistry, medicine, and industry.
J. Dove (1986)
10.1016/S1367-5931(99)80018-0
Mussel byssus and biomolecular materials.
T. Deming (1999)
10.1111/J.1399-3011.1992.TB00786.X
Circular dichroism of reduced and oxidized recombinant human epidermal growth factor.
L. Narhi (1992)
10.1016/S0960-894X(01)81162-8
5-(3-carboxymethoxyphenyl)-2-(4,5-dimethylthiazolyl)-3-(4-sulfophenyl)tetrazolium, inner salt (MTS) and related analogs of 3-(4,5-dimethylthiazolyl)-2,5-diphenyltetrazolium bromide (MTT) reducing to purple water-soluble formazans As cell-viability indicators
J. Barltrop (1991)
10.1080/00218460903291411
Salt Effects on Aggregation and Adsorption Characteristics of Recombinant Mussel Adhesive Protein fp-151
Seonghye Lim (2009)
10.1039/C7RA04228K
Molecular interactions between DOPA and surfaces with different functional groups: a chemical force microscopy study
Wei Zhang (2017)
10.1039/C7RA06743G
Mussel-inspired hydrogel tissue adhesives for wound closure
Maedeh Rahimnejad (2017)
The use of adhesives in chondrocyte transplantation surgery. Preliminary studies.
Grande Da (1988)
10.1007/BF00197809
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
F. Delaglio (1995)
10.1002/pola.28368
Recent approaches in designing bioadhesive materials inspired by mussel adhesive protein
Pegah Kord Forooshani (2017)
10.1038/327339A0
The solution structure of human epidermal growth factor
R. Cooke (1987)
10.1080/08927014.2018.1453927
Environmental post-processing increases the adhesion strength of mussel byssus adhesive
Matthew N George (2018)
10.1016/J.APMT.2017.04.001
Mussel-inspired fabrication of functional materials and their environmental applications: Progress and prospects
Xiaoyong Zhang (2017)
Molecular interactions between DOPA and sur- faces with different functional groups: a chemical force microscopy study
W. Zhang (2017)
Notch ligand -like1: X-ray crystal structure and binding affinity
N. J. Kershaw (2015)
10.1016/j.colsurfb.2011.10.037
Peptide derived from Pvfp-1 as bioadhesive on bio-inert surface.
Z. Jiang (2012)
10.1073/pnas.0605552103
Single-molecule mechanics of mussel adhesion
H. Lee (2006)
10.1242/jeb.134056
Mussel adhesion – essential footwork
J. Waite (2017)
10.1007/s10126-007-9053-x
Understanding Marine Mussel Adhesion
Heather G. Silverman (2007)
10.1063/1.1678153
Analysis of Macromolecular Polydispersity in Intensity Correlation Spectroscopy: The Method of Cumulants
D. Koppel (1972)
10.1074/JBC.270.12.6698
Mussel Adhesive Plaque Protein Gene Is a Novel Member of Epidermal Growth Factor-like Gene Family (*)
K. Inoue (1995)
10.1042/BJ20150010
Notch ligand delta-like1: X-ray crystal structure and binding affinity.
N. Kershaw (2015)
10.1021/JA990469Y
Role of l-3,4-Dihydroxyphenylalanine in Mussel Adhesive Proteins
Miaoer Yu (1999)
10.1002/POLB.22256
Natural Underwater Adhesives.
R. Stewart (2011)
10.1016/0305-0491(91)90255-C
Immunological studies of the polyphenolic proteins of mussels
C. Saez (1991)
10.1038/ncomms9737
Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins
L. Petrone (2015)
10.1016/j.str.2016.02.010
Non-Linear and Flexible Regions of the Human Notch1 Extracellular Domain Revealed by High-Resolution Structural Studies
Philip C Weisshuhn (2016)
10.1016/j.cbpa.2009.11.009
Marine bioinorganic materials: mussels pumping iron.
J. Wilker (2010)
The use of adhesives in chondro- cyte transplantation surgery: preliminary studies: bulletin of the Hospital for Joint Diseases
D. A. Grande (1988)
10.1039/c8sm00509e
Lipids as integral components in mussel adhesion.
Y. He (2018)
The use of adhesives in chondrocyte transplantation surgery. Preliminary studies.
D. Grande (1988)
10.1038/nbt.2671
Accelerating the design of biomimetic materials by integrating RNA-seq with proteomics and materials science
Paul A. Guerette (2013)
10.1038/ncomms14539
Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication
Tobias Priemel (2017)
10.1126/science.aab0556
Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement
G. Maier (2015)
Adhesion a la moule
J. H. Waite (2002)
10.2307/1542413
Characterization of a Cystine-Rich Polyphenolic Protein Family from the Blue Mussel Mytilus edulis L.
L. Rzepecki (1992)
10.1021/MA980268Z
Synthetic Polypeptide Mimics of Marine Adhesives.
Yu. (1998)
10.1016/j.biomaterials.2015.07.014
Rapidly light-activated surgical protein glue inspired by mussel adhesion and insect structural crosslinking.
Eun Young Jeon (2015)
10.1016/J.BBAPAP.2005.06.005
How to study proteins by circular dichroism.
S. Kelly (2005)



This paper is referenced by
Semantic Scholar Logo Some data provided by SemanticScholar