高雄醫學大學圖書館 |

Interfacial Properties of Therapeutic Proteins at the Air-Liquid Interface and How They Lead to Aggregation /

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Interfacial Properties of Therapeutic Proteins at the Air-Liquid Interface and How They Lead to Aggregation // Valerie P Griffin.
Author:	Griffin, Valerie P.,
Description:	1 electronic resource (268 pages)
Notes:	Source: Dissertations Abstracts International, Volume: 86-01, Section: B.
基督教聖經之智慧書導讀 :	Over the past decade, the pharmaceutical industry has seen a vast increase in the development of novel antibody-based therapeutics. However, ensuring long term stability of biologics poses a significant challenge in drug development, as they are susceptible to protein degradation caused by thermal, chemical, and/or mechanical stresses, leading to the formation of subvisible particles that can adversely impact both the safety and efficacy of the drug product. It is also now recognized that due to a protein's amphiphilic nature and tendency for interfacial adsorption, interfacial stresses encountered throughout bioprocessing and storage can lead to protein instability and protein particle formation, however the mechanisms governing interface-induced particle formation are still fundamentally lacking as these stresses are often coupled with other environmental stresses. The objective of this dissertation is to develop predictive tools to study and increase the understanding of the mechanisms leading to protein-protein interactions and their propensity to aggregate at the air-liquid interface at relevant pharmaceutical manufacturing and formulation conditions. This project will determine (1) how the interfacial properties of different monoclonal antibodies (mAbs) from protein adsorption, unfolding, and intermolecular interactions correlate to particle characterization in the bulk solution and at the air-liquid interface in response to isolated and combined environmental stresses (temperature, pH, hydrodynamic shear, interfacial dilatational stress) and (2) how differences in protein-based modalities, a mAb vs a Fusion protein, impact the formation of the protein film at the air-liquid interface over time and how this film responds to interfacial dilatational stress.
Contained By:	Dissertations Abstracts International86-01B.
Subject:	Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=30994463
ISBN:	9798383200193

Interfacial Properties of Therapeutic Proteins at the Air-Liquid Interface and How They Lead to Aggregation /
Griffin, Valerie P.,

Interfacial Properties of Therapeutic Proteins at the Air-Liquid Interface and How They Lead to Aggregation /Valerie P Griffin. - 1 electronic resource (268 pages)

Source: Dissertations Abstracts International, Volume: 86-01, Section: B.

Over the past decade, the pharmaceutical industry has seen a vast increase in the development of novel antibody-based therapeutics. However, ensuring long term stability of biologics poses a significant challenge in drug development, as they are susceptible to protein degradation caused by thermal, chemical, and/or mechanical stresses, leading to the formation of subvisible particles that can adversely impact both the safety and efficacy of the drug product. It is also now recognized that due to a protein's amphiphilic nature and tendency for interfacial adsorption, interfacial stresses encountered throughout bioprocessing and storage can lead to protein instability and protein particle formation, however the mechanisms governing interface-induced particle formation are still fundamentally lacking as these stresses are often coupled with other environmental stresses. The objective of this dissertation is to develop predictive tools to study and increase the understanding of the mechanisms leading to protein-protein interactions and their propensity to aggregate at the air-liquid interface at relevant pharmaceutical manufacturing and formulation conditions. This project will determine (1) how the interfacial properties of different monoclonal antibodies (mAbs) from protein adsorption, unfolding, and intermolecular interactions correlate to particle characterization in the bulk solution and at the air-liquid interface in response to isolated and combined environmental stresses (temperature, pH, hydrodynamic shear, interfacial dilatational stress) and (2) how differences in protein-based modalities, a mAb vs a Fusion protein, impact the formation of the protein film at the air-liquid interface over time and how this film responds to interfacial dilatational stress.

English

ISBN: 9798383200193Subjects--Topical Terms:

186550
Biochemistry.
Subjects--Index Terms:

Air-liquid Interface

Interfacial Properties of Therapeutic Proteins at the Air-Liquid Interface and How They Lead to Aggregation /
LDR:03380nam a22004453i 4500 001 391410
005 20251124054753.5
006 m o d
007 cr|nu||||||||
008 251208s2024 miu||||||m |||||||eng d
020 $a 9798383200193
035 $a (MiAaPQD)AAI30994463
035 $a AAI30994463
040 $a MiAaPQD $b eng $c MiAaPQD $e rda
100 1 $a Griffin, Valerie P., $e author. $0 (orcid)0000-0002-3585-1249 $3 523854
245 1 0 $a Interfacial Properties of Therapeutic Proteins at the Air-Liquid Interface and How They Lead to Aggregation / $c Valerie P Griffin.
264 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2024
300 $a 1 electronic resource (268 pages)
336 $a text $b txt $2 rdacontent
337 $a computer $b c $2 rdamedia
338 $a online resource $b cr $2 rdacarrier
500 $a Source: Dissertations Abstracts International, Volume: 86-01, Section: B.
500 $a Advisors: Dhar, Prajnaparamita Committee members: Gehrke, Stevin H.; Allgeier, Alan; Robinson, Jennifer; Siahaan, Teruna.
502 $b Ph.D. $c University of Kansas $d 2024.
520 $a Over the past decade, the pharmaceutical industry has seen a vast increase in the development of novel antibody-based therapeutics. However, ensuring long term stability of biologics poses a significant challenge in drug development, as they are susceptible to protein degradation caused by thermal, chemical, and/or mechanical stresses, leading to the formation of subvisible particles that can adversely impact both the safety and efficacy of the drug product. It is also now recognized that due to a protein's amphiphilic nature and tendency for interfacial adsorption, interfacial stresses encountered throughout bioprocessing and storage can lead to protein instability and protein particle formation, however the mechanisms governing interface-induced particle formation are still fundamentally lacking as these stresses are often coupled with other environmental stresses. The objective of this dissertation is to develop predictive tools to study and increase the understanding of the mechanisms leading to protein-protein interactions and their propensity to aggregate at the air-liquid interface at relevant pharmaceutical manufacturing and formulation conditions. This project will determine (1) how the interfacial properties of different monoclonal antibodies (mAbs) from protein adsorption, unfolding, and intermolecular interactions correlate to particle characterization in the bulk solution and at the air-liquid interface in response to isolated and combined environmental stresses (temperature, pH, hydrodynamic shear, interfacial dilatational stress) and (2) how differences in protein-based modalities, a mAb vs a Fusion protein, impact the formation of the protein film at the air-liquid interface over time and how this film responds to interfacial dilatational stress.
546 $a English
590 $a School code: 0099
650 4 $2 96060 $a Biochemistry. $3 186550
650 4 $a Pharmaceutical sciences. $3 523812
650 4 $2 96060 $a Bioengineering. $3 238143
650 4 $a Chemical engineering. $3 382546
653 $a Air-liquid Interface
653 $a Fc-fusion proteins
653 $a Monoclonal antibodies
653 $a Protein particle formation
653 $a Protein stability
690 $a 0542
690 $a 0202
690 $a 0572
690 $a 0487
710 2 $a University of Kansas. $b Chemical & Petroleum Engineering. $e degree granting institution. $3 523855
720 1 $a Dhar, Prajnaparamita $e degree supervisor.
773 0 $t Dissertations Abstracts International $g 86-01B.
790 $a 0099
791 $a Ph.D.
792 $a 2024
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=30994463