2021
DOI: 10.1016/j.cis.2021.102365
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Applications of serum albumins in delivery systems: Differences in interfacial behaviour and interacting abilities with polysaccharides

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Cited by 48 publications
(21 citation statements)
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“…Therefore, it can be inferred that both macrocycles are located near the Trp residue in BSA molecule [ 42 ]. It is known that the BSA molecule contains two different tryptophan residues Trp134 and Trp212, which differ significantly in their environment [ 45 ]. The interactions between BSA with 3 and 4 are additionally studied via fluorescence spectroscopy at the excitation wavelength is 295 nm.…”
Section: Resultsmentioning
confidence: 99%
“…Therefore, it can be inferred that both macrocycles are located near the Trp residue in BSA molecule [ 42 ]. It is known that the BSA molecule contains two different tryptophan residues Trp134 and Trp212, which differ significantly in their environment [ 45 ]. The interactions between BSA with 3 and 4 are additionally studied via fluorescence spectroscopy at the excitation wavelength is 295 nm.…”
Section: Resultsmentioning
confidence: 99%
“…It is known that ICG is bound to the hydrophobic core of human serum albumin, which results in some chemical stabilization of ICG [27]. BSA can act as a transporter in the body, delivering a variety of exogenous or endogenous substances, making it one of the most valued serum albumins in the biomedical field because of its high water solubility and good biocompatibility [28,29]. Thus, modification of NIR fluorescent dye ICG with BSA can increase its solubility and biocompatibility in the present study.…”
Section: Discussionmentioning
confidence: 99%
“…In other words, enough hydrophobic residues are important for protein to come together with oil phase and interact with each other to form strong interfacial film ( 16 ), while the number of hydrophilic residues determines the molecular forces between protein-water and steric hindrance within droplets (derived from dangling hydrophilic groups) ( 17 ). Briefly, a more balanced polar and nonpolar group distribution is favored for interfacial adsorption and emulsion stabilization afterward, which is determined by the protein sequence ( 18 ). Xiong et al ( 19 ) verified the pea protein isolate subunits (i.e., isoforms of vicilins) well balanced with hydrophobic and hydrophilic groups displayed better interfacial activity.…”
Section: Emulsion Related Characteristics Of Proteinmentioning
confidence: 99%