Characterization of Secondary and Tertiary Conformational Changes of β-Lactoglobulin Adsorbed on Silica Nanoparticle Surfaces

Langmuir ◽  
2008 ◽  
Vol 24 (9) ◽  
pp. 4989-4998 ◽  
Author(s):  
Xiaoyu Wu ◽  
Ganesan Narsimhan
Membranes ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 303
Author(s):  
Rokayya Sami ◽  
Schahrazad Soltane ◽  
Mahmoud Helal

In the current work, the characterization of novel chitosan/silica nanoparticle/nisin films with the addition of nisin as an antimicrobial technique for blueberry preservation during storage is investigated. Chitosan/Silica Nanoparticle/N (CH-SN-N) films presented a stable suspension as the surface loads (45.9 mV) and the distribution was considered broad (0.62). The result shows that the pH value was increased gradually with the addition of nisin to 4.12, while the turbidity was the highest at 0.39. The content of the insoluble matter and contact angle were the highest for the Chitosan/Silica Nanoparticle (CH-SN) film at 5.68%. The use of nano-materials in chitosan films decreased the material ductility, reduced the tensile strength and elongation-at-break of the membrane. The coated blueberries with Chitosan/Silica Nanoparticle/N films reported the lowest microbial contamination counts at 2.82 log CFU/g followed by Chitosan/Silica Nanoparticle at 3.73 and 3.58 log CFU/g for the aerobic bacteria, molds, and yeasts population, respectively. It was observed that (CH) film extracted 94 regions with an average size of 449.10, at the same time (CH-SN) film extracted 169 regions with an average size of 130.53. The (CH-SN-N) film presented the best result at 5.19%. It could be observed that the size of the total region of the fruit for the (CH) case was the smallest (1663 pixels), which implied that the fruit lost moisture content. As a conclusion, (CH-SN-N) film is recommended for blueberry preservation to prolong the shelf-life during storage.


2021 ◽  
pp. 004051752110238
Author(s):  
Oluwafemi P Akinmolayan ◽  
James M Manimala

Silica nanoparticle-impregnated Kevlar (SNK) fabric has better specific ballistic performance in comparison to its neat counterparts. For multifunctional structural applications using lightweight composites, combining this improved ballistic functionality with an acoustic functionality is desirable. In this study, acoustic characterization of neat and SNK samples is conducted using the normal-incidence impedance tube method. Both the absorption coefficient and transmission loss (TL) are measured in the 60–6000 Hz frequency range. The influence of parameters such as number of layers of neat or treated fabric, percentage by weight of nanoparticle addition, spacing between fabric layers, and residual porosity is examined. It is found that while absorption decreases with an increase in nanoparticle addition for frequencies above about 2500 Hz, increasing the number of layers shifts peak absorption to lower frequencies. By introducing an air-gap behind the fabric layer, dominant low-frequency (1000–3000 Hz) absorption peaks are obtained that correlate well with natural modes of mass-equivalent thin plates. Examining the influence of residual porosity by laminating the SNK samples reveals that it contributes to about 30–50% of the total absorption. Above about 1500 Hz, 3–5 dB of TL increase is obtained for SNK samples vis-à-vis the neat samples. TL is found to increase beyond that of the neat sample above a threshold frequency when an air-gap is introduced between two SNK layers. With an increase in the weight of nanoparticle addition, measured TL tends to be closer to mass law predictions. This study demonstrates that SNK fabric could provide improved acoustic performance in addition to its ballistic capabilities, making it suitable for multifunctional applications and could form the basis for the development of simplified models to predict the structural acoustic response of such nanoparticle–fabric composites.


2004 ◽  
Vol 78 (6) ◽  
pp. 2994-3002 ◽  
Author(s):  
Anne Op De Beeck ◽  
Cécile Voisset ◽  
Birke Bartosch ◽  
Yann Ciczora ◽  
Laurence Cocquerel ◽  
...  

ABSTRACT Hepatitis C virus (HCV) encodes two envelope glycoproteins, E1 and E2, that assemble as a noncovalent heterodimer which is mainly retained in the endoplasmic reticulum. Because assembly into particles and secretion from the cell lead to structural changes in viral envelope proteins, characterization of the proteins associated with the virion is necessary in order to better understand how they mature to be functional in virus entry. There is currently no efficient and reliable cell culture system to amplify HCV, and the envelope glycoproteins associated with the virion have therefore not been characterized yet. Recently, infectious pseudotype particles that are assembled by displaying unmodified HCV envelope glycoproteins on retroviral core particles have been successfully generated. Because HCV pseudotype particles contain fully functional envelope glycoproteins, these envelope proteins, or at least a fraction of them, should be in a mature conformation similar to that on the native HCV particles. In this study, we used conformation-dependent monoclonal antibodies to characterize the envelope glycoproteins associated with HCV pseudotype particles. We showed that the functional unit is a noncovalent E1E2 heterodimer containing complex or hybrid type glycans. We did not observe any evidence of maturation by a cellular endoprotease during the transport of these envelope glycoproteins through the secretory pathway. These envelope glycoproteins were recognized by a panel of conformation-dependent monoclonal antibodies as well as by CD81, a molecule involved in HCV entry. The functional envelope glycoproteins associated with HCV pseudotype particles were also shown to be sensitive to low-pH treatment. Such conformational changes are likely necessary to initiate fusion.


2017 ◽  
Vol 61 (8) ◽  
Author(s):  
David Wensel ◽  
Yongnian Sun ◽  
Zhufang Li ◽  
Sharon Zhang ◽  
Caryn Picarillo ◽  
...  

ABSTRACT A novel fibronectin-based protein (Adnectin) HIV-1 inhibitor was generated using in vitro selection. This inhibitor binds to human CD4 with a high affinity (3.9 nM) and inhibits viral entry at a step after CD4 engagement and preceding membrane fusion. The progenitor sequence of this novel inhibitor was selected from a library of trillions of Adnectin variants using mRNA display and then further optimized for improved antiviral and physical properties. The final optimized inhibitor exhibited full potency against a panel of 124 envelope (gp160) proteins spanning 11 subtypes, indicating broad-spectrum activity. Resistance profiling studies showed that this inhibitor required 30 passages (151 days) in culture to acquire sufficient resistance to result in viral titer breakthrough. Resistance mapped to the loss of multiple potential N-linked glycosylation sites in gp120, suggesting that inhibition is due to steric hindrance of CD4-binding-induced conformational changes.


2014 ◽  
Vol 132 (14) ◽  
pp. n/a-n/a ◽  
Author(s):  
Nuria Monasterio ◽  
Jose Ramon Leiza ◽  
Emiliano Meaurio ◽  
Jose Ramon Sarasua

2019 ◽  
Author(s):  
Minjoo Kim ◽  
Nicholas J. Sisco ◽  
Jacob K. Hilton ◽  
Camila M. Montano ◽  
Manuel A. Castro ◽  
...  

AbstractSensing and responding to temperature is crucial in biology. The TRPV1 ion channel is a well-studied heat-sensing receptor that is also activated by vanilloid compounds including capsaicin. Despite significant interest, the molecular underpinnings of thermosensing have remained elusive. The TRPV1 S1-S4 membrane domain couples chemical ligand binding to the pore domain during channel gating. However, the role of the S1-S4 domain in thermosensing is unclear. Evaluation of the isolated human TRPV1 S1-S4 domain by solution NMR, Far-UV CD, and intrinsic fluorescence shows that this domain undergoes a non-denaturing temperature-dependent transition with a high thermosensitivity. Further NMR characterization of the temperature-dependent conformational changes suggests the contribution of the S1-S4 domain to thermosensing shares features with known coupling mechanisms between this domain with ligand and pH activation. Taken together, this study shows that the TRPV1 S1-S4 domain contributes to TRPV1 temperature-dependent activation.


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