Polymer-antibody fragment conjugates for biomedical applications

Srivastava, Akshay; O'Connor, Iain B.; Pandit, Abhay; Wall, J. Gerard

doi:10.1016/j.progpolymsci.2013.09.003

Cited by 38 publications

(29 citation statements)

References 209 publications

(224 reference statements)

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“…[17] Understanding of the available chemical groups present on both the biomaterial surface and the protein facilitates design of chemical interactions to incorporate proteins onto the materials' surface. [32] Such proteinmaterial interactions can be highly site-specific or largely non-specific. Non-specific attachment of proteins is usually easier to carry out and considerably more efficient than siteselective binding, but the bioactivity of the tethered protein in the resultant biomaterial may be compromised.…”

Section: Attaching Proteins To Materialsmentioning

confidence: 99%

“…Commonly used chemical moieties include primary amine (-NH 2 ), carboxyl (-COOH), sulfhydryl (-SH) and carbonyl (RCOR′) groups, which are widely present in amino acids as well as in several polymeric biomaterials. [32] Chemical conjugation approaches have gained considerably in popularity for biomaterial functionalization due to the higher stability of protein tethering and, importantly, their potential to correctly orient proteins on the surface for increased activity (Figure 3).…”

Section: Covalent Modification Techniquesmentioning

confidence: 99%

“…One approach is to utilize Fc-binding proteins to ensure accessibility of the antigen binding pocket upon surface attachment of the antibody [172] but incorporation of this additional protein layer has the potential to increase non-specific interaction events and even to elicit undesired immune responses in vivo in the case of antibody-binding proteins derived from bacteria. [172b] Other approaches to improve antibody immobilization [32,173] include the oxidation of naturally occurring oligosaccharide chains in the Fc stem of whole antibodies followed by their covalent linking to surface amine groups. [174] This method has also been utilized with glycoengineered scFv fragments produced in E. coli with a non-native sugar chain.…”

Section: Progress Reportmentioning

confidence: 99%

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Adding Functions to Biomaterial Surfaces through Protein Incorporation

et al. 2016

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The concept of biomaterials has evolved from one of inert mechanical supports with a long-term, biologically inactive role in the body into complex matrices that exhibit selective cell binding, promote proliferation and matrix production, and may ultimately become replaced by newly generated tissues in vivo. Functionalization of material surfaces with biomolecules is critical to their ability to evade immunorecognition, interact productively with surrounding tissues and extracellular matrix, and avoid bacterial colonization. Antibody molecules and their derived fragments are commonly immobilized on materials to mediate coating with specific cell types in fields such as stent endothelialization and drug delivery. The incorporation of growth factors into biomaterials has found application in promoting and accelerating bone formation in osteogenerative and related applications. Peptides and extracellular matrix proteins can impart biomolecule- and cell-specificities to materials while antimicrobial peptides have found roles in preventing biofilm formation on devices and implants. In this progress report, we detail developments in the use of diverse proteins and peptides to modify the surfaces of hard biomaterials in vivo and in vitro. Chemical approaches to immobilizing active biomolecules are presented, as well as platform technologies for isolation or generation of natural or synthetic molecules suitable for biomaterial functionalization.

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Section: Attaching Proteins To Materialsmentioning

confidence: 99%

Section: Covalent Modification Techniquesmentioning

confidence: 99%

Section: Progress Reportmentioning

confidence: 99%

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Adding Functions to Biomaterial Surfaces through Protein Incorporation

et al. 2016

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“…However, due to high endogenous levels of transferrin nearly saturating the receptors, antibodies against the transferrin receptor, that do not compete with transferrin binding, such as OX26 (rat) and RI7217 (mouse) offer practical alternatives for in vivo studies [113,114]. Research has also turned toward the use of antibody fragments to functionalize polymers [98], due to the improved tissue penetration, reduced immunogenicity, or increased packing density of these small fragments compared to the parent molecule [115]. Immunoliposomes targeted with the OX26 antibody showed greater gene delivery than non-targeted liposomes [113], while in a comparative study RI7217 targeted liposomes showed better brain uptake than four other targeting moieties [114].…”

Section: Adding Functionality (Targeting Cell Entry Etc)mentioning

confidence: 99%

Prospects for polymer therapeutics in Parkinson's disease and other neurodegenerative disorders

Newland

Werner

et al. 2015

Progress in Polymer Science

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a b s t r a c tParkinson's disease (PD) is characterized by a progressive loss of dopaminergic neurons and represents a growing health burden to western societies. Like many neurodegenerative disorders the cause is unknown, however, as the pathogenesis becomes ever more elucidated, it is becoming clear that effective delivery is a key issue for new therapeutics. The versatility of today's polymerization techniques allows the synthesis of a wide range of polymer materials which hold great potential to aid in the delivery of small molecules, proteins, genetic material or cells. In this review, we capture the recent advances in polymer based therapeutics of the central nervous system (CNS). We place the advances in historical context and, furthermore, provide future prospects in line with newly discovered advancements in the understanding of PD and other neurodegenerative disorders. This review provides researchers in the field of polymer chemistry and materials science an up-to-date understanding of the requirements placed upon materials designed for use in the CNS aiding the focus of polymer therapeutic design.

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“…[1–3] Synthetic bioconjugates often contain diverse functionality that allow them to be used as biomarker-specific imaging agents, tagged or immobilized constructs for a variety of affinity assays, as well as selective drug delivery systems. [3–7] However, the demands of reaction rate and chemoselectivity often require compromises on the covalent nature of the linkage which is often large and/or hydrophobic. As a result, conjugation chemistries that yield a structurally desirable linkage while maintaining chemoselectivity have enhanced utility.…”

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confidence: 99%

Adapting the Glaser Reaction for Bioconjugation: Robust Access to Structurally Simple, Rigid Linkers

2017

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The copper-mediated coupling between alkynes to generate a structurally rigid, linear 1,3-diyne linkage has been known for over a century. However, the mechanistic requirement to simultaneously maintain Cu(I) and an oxidant has limited its practical utility, especially for complex functional molecules in aqueous solution. We find that addition of a specific bpy-diol ligand protects unprotected peptides from Cu(II) mediated oxidative damage through formation of an insoluble Cu(II) gel which solves the critical challenge of applying the Glaser coupling to substrates that are degraded by Cu(II). The generality of this method is illustrated through conjugation of a series of polar and nonpolar labels onto a fully unprotected GLP-1R agonist through a linear 7 Å diynyl linker.

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Polymer-antibody fragment conjugates for biomedical applications

Cited by 38 publications

References 209 publications

Adding Functions to Biomaterial Surfaces through Protein Incorporation

Adding Functions to Biomaterial Surfaces through Protein Incorporation

Prospects for polymer therapeutics in Parkinson's disease and other neurodegenerative disorders

Adapting the Glaser Reaction for Bioconjugation: Robust Access to Structurally Simple, Rigid Linkers

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