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Does the protein corona take over the selectivity of molecularly imprinted nanoparticles? The biological challenges to recognition.
Capriotti, Annalaura; Piovesana, Susy; Zenezini Chiozzi, Riccardo; Montone, Carmela Maria; Bossi, Alessandra Maria; Laganà, Aldo.
  • Capriotti A; University of Rome "La Sapienza", Department of Chemistry, Piazzale Aldo Moro 5, 00185 Rome, Italy.
  • Piovesana S; University of Rome "La Sapienza", Department of Chemistry, Piazzale Aldo Moro 5, 00185 Rome, Italy.
  • Zenezini Chiozzi R; University of Rome "La Sapienza", Department of Chemistry, Piazzale Aldo Moro 5, 00185 Rome, Italy.
  • Montone CM; University of Rome "La Sapienza", Department of Chemistry, Piazzale Aldo Moro 5, 00185 Rome, Italy.
  • Bossi AM; University of Verona, Department of Biotechnology, Strada Le Grazie 15, 37134 Verona, Italy. Electronic address: alessandramaria.bossi@univr.it.
  • Laganà A; University of Rome "La Sapienza", Department of Chemistry, Piazzale Aldo Moro 5, 00185 Rome, Italy.
J Proteomics ; 219: 103736, 2020 05 15.
Article in English | MEDLINE | ID: covidwho-276943
Semantic information from SemMedBD (by NLM)
1. Protein Corona compared_with Particle
Subject
Protein Corona
Predicate
compared_with
Object
Particle
2. Protein Corona higher_than Particle
Subject
Protein Corona
Predicate
higher_than
Object
Particle
3. Plasma specimen LOCATION_OF Immunoglobulins
Subject
Plasma specimen
Predicate
LOCATION_OF
Object
Immunoglobulins
4. Protein Corona compared_with Proteins
Subject
Protein Corona
Predicate
compared_with
Object
Proteins
5. Protein Corona higher_than Proteins
Subject
Protein Corona
Predicate
higher_than
Object
Proteins
6. Proteins COEXISTS_WITH Protein Corona
Subject
Proteins
Predicate
COEXISTS_WITH
Object
Protein Corona
7. Protein Corona compared_with Particle
Subject
Protein Corona
Predicate
compared_with
Object
Particle
8. Protein Corona higher_than Particle
Subject
Protein Corona
Predicate
higher_than
Object
Particle
9. Plasma specimen LOCATION_OF Immunoglobulins
Subject
Plasma specimen
Predicate
LOCATION_OF
Object
Immunoglobulins
10. Protein Corona compared_with Proteins
Subject
Protein Corona
Predicate
compared_with
Object
Proteins
11. Protein Corona higher_than Proteins
Subject
Protein Corona
Predicate
higher_than
Object
Proteins
12. Proteins COEXISTS_WITH Protein Corona
Subject
Proteins
Predicate
COEXISTS_WITH
Object
Protein Corona
ABSTRACT
"Plastic antibodies" are nano-sized biomimetics prepared by the molecular imprinting technology, which have the robustness of polymers, but specificity and selectivity alike natural receptors making them ideal for analytical uses. The current challenge is to translate plastic antibodies to in vivo applications for diagnosis, drug delivery, theranostic, therefore it is crucial to evaluate the effect of the biological sample complexity on the selectivity and the formation of protein corona (PCs), which ultimately dictate the fate of circulating nanoparticles. A set (n = 4) of plastic antibodies (nanoMIPs) against different proteins was prepared. Quantitative (iBAC) shotgun proteomics permitted to define the PC composition of nanoMIPs in human plasma, the relative protein abundances, the correlation between PC and the plasma dilution. NanoMIPs showed >200 proteins PC, while ~150 proteins were found on controls, suggesting the imprinting process influences the nanoparticle's structure hence the protein uptake. NanoMIPs and controls shared the 44% of the PC, but PC iBAQ values on nanoMIPs were 10-100 times higher than controls, suggesting PC/nanoMIPs interactions were far stronger than PC/non imprinted particles. PCs were richer in small proteins and in immunoglobulins, indicating a defensive response, while the selectivity was negatively challenged in the crowded plasma sample.

SIGNIFICANCE:

The formation and the composition of the protein corona (PC) is key to decide the fate of nanoparticles when in vivo, therefore there is the strong need to study the composition of the PC. To enable and to support the translation of the use of plastic antibodies (nanoMIPs), prepared by means of the molecular imprinting technique, to the clinical practice and to in vivo uses, the present work evaluates the effects of the complexity of the biological sample (plasma) on nanoMIPs composed of highly crosslinked polyacrylamide and acrylamide derivatives. Proteomic study offers an in depth insight of the protein corona formed in plasma on nanoMIPs. A set of nanoMIPs synthesized and raised to recognize either small or large proteins was tested. The selection abilities of the nanoMIPs when placed in plasma at different dilutions was studied. Quantitative shotgun proteomics allowed to define the composition of the formed protein corona (PC) enabling to detail the protein compositions, the relative abundances, its correlation to the biological sample composition and the correlation between PC and nanoMIP's imprinted template. In plasma, all the nanoMIPs gained a PC composed of more than 200 proteins. Type of protein recruited for the corona, molecular weight and abundance in the PC were studied. The PC on the nanoMIPs appeared to be driven by the protein composition of the plasma, while the template protein, towards which a nanoMIP was imprinted and that was proven to have high affinity for, did not influence the PC.
Subject(s)

Full text: Available Collection: International databases Database: MEDLINE Main subject: Nanoparticles / Molecular Imprinting / Protein Corona Limits: Humans Language: English Journal: J Proteomics Journal subject: Biochemistry Year: 2020 Document Type: Article Affiliation country: J.jprot.2020.103736

Full text: Available Collection: International databases Database: MEDLINE Main subject: Nanoparticles / Molecular Imprinting / Protein Corona Limits: Humans Language: English Journal: J Proteomics Journal subject: Biochemistry Year: 2020 Document Type: Article Affiliation country: J.jprot.2020.103736