title: Fabrication of collagen-elastin-bound peptide microtubes for mammalian cell attachment.
abstract: In this work we have designed self-assembled peptide-based microconstructs and examined their interactions with elastin and collagen for potential application as scaffolds for chondrocyte cell attachment. Being biological in nature, peptide-based nano- and microstructures have intrinsic molecular recognition properties which allow extensive chemical, conformational and functional diversity. We have synthesized a new peptide bolaamphiphile, bis(N-α-amido-val)-1,5-pentane dicarboxylate, and examined its self-assembly at varying pH values. The formation of high-density networks of nano- and microtubular structures was found to be in the range of pH 4-6. The formed microtubes were then covalently bound to varying concentrations of the extracellular matrix protein elastin, a versatile protein that allows for an extensive array of physical and chemical modifications to attune properties towards diverse necessities of biomedical applications. We found that binding to microtubes was concentration dependent. The morphological and chemical changes complementing the processes of self-assembly and binding to elastin were examined by electron microscopic and spectroscopic methods. Furthermore, we also incorporated the extracellular matrix protein type-I collagen, a critical constituent for designing biocompatible scaffolds, into the elastin functionalized micro-tubes. Since the main goal is to develop highly biocompatible protein functionalized microstructures that support cellular interactions, we examined the interactions of the microcomposites with chondrocyte cell line, in order to assess the biocompatibility and interaction between the microconstructs and the cells. The designed elastin and collagen-bound peptide microtubes may potentially serve as a new class of biomaterials by promoting cell growth and proliferation.
authors.affiliation: a Department of Chemistry , Fordham University , 441 East Fordham Road, Bronx , New York , NY , 10458 , USA.
authors.forename: Nako
authors.initials: N
authors.lastname: Nakatsuka
authors.forename: Stacey N
authors.initials: SN
authors.lastname: Barnaby
authors.forename: Karl R
authors.initials: KR
authors.lastname: Fath
authors.forename: Ipsita A
authors.initials: IA
authors.lastname: Banerjee
mesh_terms: D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry; D001826:Body Fluids; D002448:Cell Adhesion / Q000502:physiology*; D002460:Cell Line; D019902:Chondrocytes / Q000502:physiology; D024042:Collagen Type I / Q000737:chemistry; D004549:Elastin / Q000737:chemistry; D005663:Furans / Q000138:chemical synthesis / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008422:Materials Testing; D018625:Microscopy, Atomic Force; D008855:Microscopy, Electron, Scanning; D046529:Microscopy, Electron, Transmission; D015394:Molecular Structure; D049329:Nanostructures / Q000737:chemistry; D011728:Pyridones / Q000138:chemical synthesis / Q000737:chemistry; D011817:Rabbits; D017550:Spectroscopy, Fourier Transform Infrared; D054457:Tissue Scaffolds / Q000737:chemistry
chemical_list: D001672:Biocompatible Materials; D024042:Collagen Type I; D005663:Furans; D011728:Pyridones; C543575:bolaamphiphile; D004549:Elastin