FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2093023654> ?p ?o ?g. }

• W2093023654 endingPage "1907" @default.
• W2093023654 startingPage "1905" @default.
• W2093023654 abstract "NanomedicineVol. 9, No. 13 EditorialFree AccessGold nanoparticles: testbeds for engineered protein–particle interactionsDaniel F Moyano & Vincent M RotelloDaniel F MoyanoDepartment of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, MA 01003, USASearch for more papers by this author & Vincent M RotelloAuthor for correspondence: E-mail Address: rotello@chem.umass.eduDepartment of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, MA 01003, USASearch for more papers by this authorPublished Online:24 Oct 2014https://doi.org/10.2217/nnm.14.114AboutSectionsPDF/EPUB ToolsAdd to favoritesDownload CitationsTrack CitationsPermissionsReprints ShareShare onFacebookTwitterLinkedInRedditEmail Keywords: enzymatic activityfunctionalized gold nanoparticlesnonfouling propertiesprotein coronaprotein stabilityself-assembled monolayersstealth nanoparticlesControlling the interactions of nanoparticles with biosystems is crucial for using these materials in diagnostic, imaging and therapeutic applications. Interfacing nanoparticles with proteins is an important issue for each of these applications. In diagnostic applications, for example, the ability to recognize proteins provides access to sensor systems for quantifying biomarkers and profiling complex biofluids [1]. Protein recognition is similarly important in therapeutic and imaging applications, where the interaction with specific markers is a desirable feature. Equally essential for all of these cases is the ability to turn off interactions (i.e., creating ‘stealth’ nanoparticles) [2]. On the sensing side, noninteracting coatings can be used to enhance specificity and prevent biofouling. With diagnostics and imaging agents, stealth coatings can be used to help evade immune responses – especially since neutralizing nanoscale objects (e.g., bacteria and viruses) is a central goal of the immune system.Along with the promise of engineered nanoparticle–protein interactions come multiple challenges. First, there is an enormous spectrum of protein sizes, charges, hydrophobicities and other parameters that need to be considered when engineering the interface [3]. Second, proteins are at very high concentrations in biofluids (e.g., ˜1 mM in human serum). This high concentration means that even rather weak interactions will complicate desired recognition events. Third, and perhaps most daunting of all, is that protein structures are highly dynamic and can be readily distorted and even denatured through binding events [4].Gold nanoparticles (AuNPs) provide a particularly useful platform for engineering and studying biointeractions [5]. The surfaces of these particles can be readily and stably tuned using thiol-based ligands that bind strongly to the gold surface. For smaller particles (≤6–8-nm core diameter), well-formed monolayers can be generated, providing chemical control of the surface through the generation of homogeneous and mixed monolayer particles [6]. Larger particles can be similarly functionalized; however, their surface structure is by nature less regular, featuring ligands and ionic species at the surface. Next, elemental gold is nontoxic, meaning that the lessons we learn with AuNPs can be directly translated to real-world applications [7]. Finally, our experience has shown that AuNPs are frankly the easiest particles to make in a stable form in useful quantities.The creation of noninteracting particles is a challenge that has continued over decades of research [8]. This long and difficult problem is due at least in part to the fact that ‘noninteracting’ is an ideal, not a reality. When thinking of materials in complex biofluids, it helps to think of a very crowded party – one where you will continually bump into people. The key to navigating both parties and serum is to minimize the interaction time, avoiding sticky and undesirable interactions that would result in aggregation.The traditional way of generating stealth particles is through the use of PEG ligands [2,9]. Although PEG has been employed widely both in vitro and in vivo, there are two limitations to this approach. First, PEG is uncharged, making it challenging to engineer the desired electrostatic and hydrophobic interactions [10]. This issue has been addressed with smaller AuNPs that require commensurately short PEG units. Small AuNPs (2–6-nm core diameter) can be functionalized with short PEG units (e.g., tetraethylene glycol) that allow functionality to be synthetically placed at the ligand terminus [11]. Other particles can be functionalized with longer PEG chains in mixed monolayer AuNPs.While PEG functionalization has been widely employed with nanomaterials and works well for ex vivo applications, recent studies have shown that PEG chains of different sizes will elicit the formation of antibodies [12]. This immune response is actually quite a problem, resulting in complement activation that can generate a range of physiological reactions, including anaphylactic shock. Fortunately, self-complementary cation–anion pairs (i.e., zwitterions [9]) have been shown to have excellent resistance to protein fouling, and have recently been shown to be nonimmunogenic [13].As mentioned above, nanoparticle–protein interactions will always be present in serum and in cells. A complicating feature of these interactions is that proteins will tend to alter their structure in order to optimize their interactions with surfaces. This denaturation process converts reversible protein–particle interactions into irreversible states, generating a protein coat that has been termed the ‘protein corona’ [14]. This corona can mask desired interactions, as well as foster immune response and induce aggregation. While many researchers feel that the generation of this corona is inevitable, appropriate engineering of the particle monolayer in order to foster reversible protein–particle interactions provides a path to avoiding irreversible fouling interactions with the concomitant formation of permanent coronas [15].Clearly, generating particles that bind proteins reversibly would be helpful for delivery. Controlled interactions of this sort are a requirement in applications in which delivery of the active protein/enzyme is essential and targeting functionalities may be masked by proteins that have been adsorbed in a nonreversible fashion [16]. Reversible binding is also crucial for sensing, where denaturation results in sensor fouling and inactivity.Initial studies of protein–particle interactions using amphiphilic particles resulted in protein denaturation at the particle surface, generating the widely held belief that denaturation is inevitable at particle surfaces. This assumption is quite incorrect – nanoparticles have been engineered to stabilize the protein structure, maintaining and even enhancing activity [17]. AuNPs have been particularly successful in this regard in applications requiring the maintenance of protein structure, including sensing, delivery and even ‘green chemistry’ strategies using biocatalysts.What are the secrets to generating reversible protein–particle interactions? First, size is an important parameter. Smaller particles are better at preventing denaturation for a variety of reasons, particularly the radius of curvature [18]. Second, amphiphilicity must be handled very carefully – there is a strong energetic push for hydrophobic protein residues to interact with hydrophobic surfaces. That is not to say that all greasiness is bad, as AuNPs with hydrophobic head groups were found to maintain protein structure better than purely hydrophilic analogs [19]. Finally, ligand flexibility is crucial – if the particle cannot adapt to the protein, the protein will adapt (i.e., denature) to the particle.Small AuNPs provide an excellent platform for providing all of the above attributes. In addition to their demonstrated utility in applications, the nature of this AuNP–protein interaction has been explored using calorimetry [20]. This study demonstrated that 2-nm core AuNPs with appropriate surfaces effectively mimic protein–protein interactions, making these particles, in essence, artificial proteins.Taken together, we have come a long way in understanding and engineering particle–protein interactions, with a large proportion of the insights being provided by AuNPs. We have some answers regarding how to generate noninteracting particles, and some demonstrated successes in generating reversible particle–protein interactions. However, all of these insights relate to specific systems. What remains is to convert the one-off insights of individual studies into general engineering principles. Once this goal has been achieved, we will have a truly ‘plug-and-play’ playbook for creating protein–nanoparticle bioconjugates.Financial & competing interests disclosureVM Rotello acknowledges support from the NIH (EB014277 and GM077173). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.No writing assistance was utilized in the production of this manuscript.References1 Saha K, Agasti SS, Kim C, Li X, Rotello VM. Gold nanoparticles in chemical and biological sensing. Chem. Rev. 112, 2739–2779 (2012).Crossref, Medline, CAS, Google Scholar2 Jokerst JV, Lobovkina T, Zare RN, Gambhir SS. Nanoparticle PEGylation for imaging and therapy. Nanomedicine 6, 715–728 (2011).Link, CAS, Google Scholar3 De M, Miranda OR, Rana S, Rotello VM. Size and geometry dependent protein–nanoparticle self-assembly. Chem. Commun. 2157–2159 (2009).Crossref, Medline, Google Scholar4 Nel AE, Mädler L, Velegol D et al. Understanding biophysicochemical interactions at the nano–bio interface. Nat. Mater. 8, 543–557 (2009).Crossref, Medline, CAS, Google Scholar5 Weintraub K. Biomedicine: the new gold standard. Nature 495, S14–S16 (2013).Crossref, Medline, CAS, Google Scholar6 Moyano DF, Rotello VM. Nano meets biology: structure and function at the nanoparticle interface. Langmuir 27, 10376–10385 (2011).Crossref, Medline, CAS, Google Scholar7 Alkilany AM, Murphy CJ. Toxicity and cellular uptake of gold nanoparticles: what we have learned so far? J. Nanopart. Res. 12, 2313–2333 (2010).Crossref, Medline, CAS, Google Scholar8 Hoffman AS. The origins and evolution of ‘controlled’ drug delivery systems. J. Control. Release 132, 153–163 (2008).Crossref, Medline, CAS, Google Scholar9 Cao Z, Jiang S. Super-hydrophilic zwitterionic poly(carboxybetaine) and amphiphilic non-ionic poly(ethylene glycol) for stealth nanoparticles. Nano Today 7, 404–413 (2012).Crossref, CAS, Google Scholar10 Sekiguchi S, Niikura K, Matsuo Y, Ijiro K. Hydrophilic gold nanoparticles adaptable for hydrophobic solvents. Langmuir 28, 5503–5507 (2012).Crossref, Medline, CAS, Google Scholar11 You C-C, De M, Rotello VM. Contrasting effects of exterior and interior hydrophobic moieties in the complexation of amino acid functionalized gold clusters with α-chymotrypsin. Org. Lett. 7, 5685–5688 (2005).Crossref, Medline, CAS, Google Scholar12 Wang XY, Ishida T, Kiwada H. Anti-PEG IgM elicited by injection of liposomes is involved in the enhanced blood clearance of a subsequent dose of PEGylated liposomes. J. Control. Release 119, 236–244 (2007).Crossref, Medline, CAS, Google Scholar13 Yang W, Liu S, Bai T et al. Poly(carboxybetaine) nanomaterials enable long circulation and prevent polymer-specific antibody production. Nano Today 9, 10–16 (2014).Crossref, CAS, Google Scholar14 Lynch I, Dawson KA. Protein–nanoparticle interactions. Nano Today 3, 40–47 (2008).Crossref, CAS, Google Scholar15 Casals E, Puntes VF. Inorganic nanoparticle biomolecular corona: formation, evolution and biological impact. Nanomedicine 7, 1917–1930 (2012).Link, CAS, Google Scholar16 Liu R, Kay BK, Jiang S, Chen S. Nanoparticle delivery: targeting and nonspecific binding. MRS Bull. 34, 432–440 (2009).Crossref, CAS, Google Scholar17 You C-C, Agasti SS, De M, Knapp MJ, Rotello VM. Modulation of the catalytic behavior of α-chymotrypsin at monolayer-protected nanoparticle surfaces. J. Am. Chem. Soc. 128, 14612–14618 (2006).Crossref, Medline, CAS, Google Scholar18 Shang W, Nuffer JH, Muñiz-Papandrea VA et al. Cytochrome C on silica nanoparticles: influence of nanoparticle size on protein structure, stability, and activity. Small 5, 470–476 (2009).Crossref, Medline, CAS, Google Scholar19 You C-C, De M, Han G, Rotello VM. Tunable inhibition and denaturation of α-chymotrypsin with amino acid-functionalized gold nanoparticles. J. Am. Chem. Soc. 127, 12873–12881 (2005).Crossref, Medline, CAS, Google Scholar20 De M, You C-C, Srivastava S, Rotello VM. Biomimetic interactions of proteins with functionalized nanoparticles: a thermodynamic study. J. Am. Chem. Soc. 129, 10747–10753 (2007).Crossref, Medline, CAS, Google ScholarFiguresReferencesRelatedDetailsCited BySTRUCTURAL AND FUNCTIONAL INTERDEPENDENCES OF BIOLOGICAL ORGANISMS IN EXTREME CONDITIONS30 December 2022 | Biotechnologia Acta, Vol. 15, No. 6Effect of the ligand’s bulkiness on the shape of functionalized gold nanoparticles in aqueous solutions: A molecular dynamics studyChemical Physics Letters, Vol. 731Low-Resolution Models for the Interaction Dynamics of Coated Gold Nanoparticles with β2-microglobulin8 August 2019 | International Journal of Molecular Sciences, Vol. 20, No. 16Paramagnetic Nanoparticles Leave Their Mark on Nuclear Spins of Transiently Adsorbed Proteins22 December 2015 | Journal of the American Chemical Society, Vol. 138, No. 1 Vol. 9, No. 13 STAY CONNECTED Metrics History Published online 24 October 2014 Published in print September 2014 Information© Future Medicine LtdKeywordsenzymatic activityfunctionalized gold nanoparticlesnonfouling propertiesprotein coronaprotein stabilityself-assembled monolayersstealth nanoparticlesFinancial & competing interests disclosureVM Rotello acknowledges support from the NIH (EB014277 and GM077173). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.No writing assistance was utilized in the production of this manuscript.PDF download" @default.
• W2093023654 created "2016-06-24" @default.
• W2093023654 creator A5028730940 @default.
• W2093023654 creator A5076949431 @default.
• W2093023654 date "2014-09-01" @default.
• W2093023654 modified "2023-10-16" @default.
• W2093023654 title "Gold nanoparticles: testbeds for engineered protein–particle interactions" @default.
• W2093023654 cites W1973254329 @default.
• W2093023654 cites W1973681903 @default.
• W2093023654 cites W1975828910 @default.
• W2093023654 cites W1982074128 @default.
• W2093023654 cites W2014960272 @default.
• W2093023654 cites W2016107861 @default.
• W2093023654 cites W2017962752 @default.
• W2093023654 cites W2020451212 @default.
• W2093023654 cites W2032505506 @default.
• W2093023654 cites W2042994271 @default.
• W2093023654 cites W2054371878 @default.
• W2093023654 cites W2081237883 @default.
• W2093023654 cites W2082370264 @default.
• W2093023654 cites W2088344114 @default.
• W2093023654 cites W2090241203 @default.
• W2093023654 cites W2091247188 @default.
• W2093023654 cites W2106878780 @default.
• W2093023654 cites W2107910518 @default.
• W2093023654 cites W2158558808 @default.
• W2093023654 cites W2314694804 @default.
• W2093023654 doi "https://doi.org/10.2217/nnm.14.114" @default.
• W2093023654 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25343345" @default.
• W2093023654 hasPublicationYear "2014" @default.
• W2093023654 type Work @default.
• W2093023654 sameAs 2093023654 @default.
• W2093023654 citedByCount "4" @default.
• W2093023654 countsByYear W20930236542015 @default.
• W2093023654 countsByYear W20930236542019 @default.
• W2093023654 countsByYear W20930236542022 @default.
• W2093023654 crossrefType "journal-article" @default.
• W2093023654 hasAuthorship W2093023654A5028730940 @default.
• W2093023654 hasAuthorship W2093023654A5076949431 @default.
• W2093023654 hasBestOaLocation W20930236541 @default.
• W2093023654 hasConcept C104819515 @default.
• W2093023654 hasConcept C155672457 @default.
• W2093023654 hasConcept C171250308 @default.
• W2093023654 hasConcept C18903297 @default.
• W2093023654 hasConcept C192562407 @default.
• W2093023654 hasConcept C2778517922 @default.
• W2093023654 hasConcept C86803240 @default.
• W2093023654 hasConceptScore W2093023654C104819515 @default.
• W2093023654 hasConceptScore W2093023654C155672457 @default.
• W2093023654 hasConceptScore W2093023654C171250308 @default.
• W2093023654 hasConceptScore W2093023654C18903297 @default.
• W2093023654 hasConceptScore W2093023654C192562407 @default.
• W2093023654 hasConceptScore W2093023654C2778517922 @default.
• W2093023654 hasConceptScore W2093023654C86803240 @default.
• W2093023654 hasIssue "13" @default.
• W2093023654 hasLocation W20930236541 @default.
• W2093023654 hasLocation W20930236542 @default.
• W2093023654 hasOpenAccess W2093023654 @default.
• W2093023654 hasPrimaryLocation W20930236541 @default.
• W2093023654 hasRelatedWork W1624797 @default.
• W2093023654 hasRelatedWork W1659871537 @default.
• W2093023654 hasRelatedWork W1949678770 @default.
• W2093023654 hasRelatedWork W1982563407 @default.
• W2093023654 hasRelatedWork W2024714805 @default.
• W2093023654 hasRelatedWork W2166863655 @default.
• W2093023654 hasRelatedWork W2313463429 @default.
• W2093023654 hasRelatedWork W2315962575 @default.
• W2093023654 hasRelatedWork W2558431542 @default.
• W2093023654 hasRelatedWork W3114424702 @default.
• W2093023654 hasVolume "9" @default.
• W2093023654 isParatext "false" @default.
• W2093023654 isRetracted "false" @default.
• W2093023654 magId "2093023654" @default.
• W2093023654 workType "article" @default.