Functional protein to polymer surfaces: an attachment

Abstract The attachment of proteins to polymers alters the properties of every unit and paves the way to several new applications. Protein attachment behavior has achieved tremendous attention in the last few years and is largely controlled by surface characteristics. Three main routes are available for synthesizing protein–polymer conjugates and the interaction forces between protein molecules and polymer particles are mainly hydrophobic interaction, ionic (or electrostatic) bonding, hydrogen bonding and van der Waals interactions. Many chemical strategies have been developed to couple the different synthetic polymers onto the proteins. Surface modification plays a critical role in the effectiveness of activated materials and is achieved by the physical and chemical methods. The classes of the functional groups present on the protein surfaces showing various possible reactions derives from the selected amino acid residues. Attachment of the proteins with the polymer chains are based on ten natural amino acids which are available for ligation chemistry and novel nonnatural moieties. The synergistic combination of the properties has led to certain advantages in bio-applications. This chapter highlighted different routes towards protein–polymer attachment which requires a careful selection of the right chemistry that is most suitable for a respective attachment.