BiointerphasesPub Date : 2023-05-01DOI: 10.1116/6.0002613
Hyun Kyong Shon, Jin Gyeong Son, Sun Young Lee, Jeong Hee Moon, Ga Seul Lee, Kyoung-Shim Kim, Tae Geol Lee
{"title":"Comparison study of mouse brain tissue by using ToF-SIMS within static limits and hybrid SIMS beyond static limits (dynamic mode).","authors":"Hyun Kyong Shon, Jin Gyeong Son, Sun Young Lee, Jeong Hee Moon, Ga Seul Lee, Kyoung-Shim Kim, Tae Geol Lee","doi":"10.1116/6.0002613","DOIUrl":"https://doi.org/10.1116/6.0002613","url":null,"abstract":"<p><p>In the study of degenerative brain diseases, changes in lipids, the main component of neurons, are particularly important because they are used as indicators of pathological changes. One method for the sensitive measurement of biomolecules, especially lipids, is time-of-flight secondary ion mass spectrometry (ToF-SIMS) using pulsed argon cluster ions. In this study, biomolecules including various lipids present in normal mouse brain tissue were measured using ToF-SIMS equipped with pulsed argon cluster primary ions. Based on the ToF-SIMS measurement results, hybrid SIMS (OrbiSIMS), which is a ToF-SIMS system with the addition of an orbitrap mass analyzer, was used to directly identify the biomolecules by the region in the real tissue samples. For this, the results of ToF-SIMS, which measured the tissue samples from a single mouse brain within static limits, were compared with those from OrbiSIMS measured beyond the static limits in terms of the differences in molecular profiling. From this analysis, two types of positive and negative ions were selected for identification, with the OrbiSIMS MS/MS results indicating that the positive ions were glycerophosphocholine and the negative ions were glycerophosphoinositol and sulfatide, a sphingolipid. Then, to confirm the identification of the molecular candidates, lipids were extracted from mirror image tissue samples, and LC-MS/MS also using an orbitrap mass analyzer was performed. As a result, the direct identification of molecular candidate groups distributed in particular regions of the tissue samples via OrbiSIMS was found to be consistent with the identification results by LC-MS/MS for extracted samples.</p>","PeriodicalId":9053,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2023-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9981325","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BiointerphasesPub Date : 2023-05-01DOI: 10.1116/6.0002712
Ze-Qun Zhang, Ke-Feng Ren, Jian Ji
{"title":"Silane coupling agent in biomedical materials.","authors":"Ze-Qun Zhang, Ke-Feng Ren, Jian Ji","doi":"10.1116/6.0002712","DOIUrl":"https://doi.org/10.1116/6.0002712","url":null,"abstract":"<p><p>Medical devices are becoming more and more significant in our daily life. For implantable medical devices, good biocompatibility is required for further use in vivo. Thus, surface modification of medical devices is really important, which gives a wide application scene for a silane coupling agent. The silane coupling agent is able to form a durable bond between organic and inorganic materials. The dehydration process provides linking sites to achieve condensation of two hydroxyl groups. The forming covalent bond brings excellent mechanical properties among different surfaces. Indeed, the silane coupling agent is a popular component in surface modification. Metals, proteins, and hydrogels are using silane coupling agent to link parts commonly. The mild reaction environment also brings advantages for the spread of the silane coupling agent. In this review, we summarize two main methods of using the silane coupling agent. One is acting as a crosslinker mixed in the whole system, and the other is to provide a bridge between different surfaces. Moreover, we introduce their applications in biomedical devices.</p>","PeriodicalId":9053,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2023-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10411936","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BiointerphasesPub Date : 2023-05-01DOI: 10.1116/6.0002640
M Eremchev, D Roesel, P-M Dansette, A Michailovas, S Roke
{"title":"High throughput wide field second harmonic imaging of giant unilamellar vesicles.","authors":"M Eremchev, D Roesel, P-M Dansette, A Michailovas, S Roke","doi":"10.1116/6.0002640","DOIUrl":"10.1116/6.0002640","url":null,"abstract":"<p><p>Cell-sized giant unilamellar vesicles (GUVs) are an ideal tool for understanding lipid membrane structure and properties. Label-free spatiotemporal images of their membrane potential and structure would greatly aid the quantitative understanding of membrane properties. In principle, second harmonic imaging is a great tool to do so, but the low degree of spatial anisotropy that arises from a single membrane limits its application. Here, we advance the use of wide-field high throughput SH imaging by SH imaging with the use of ultrashort laser pulses. We achieve a throughput improvement of 78% of the maximum theoretical value and demonstrate subsecond image acquisition times. We show how the interfacial water intensity can be converted into a quantitative membrane potential map. Finally, for GUV imaging, we compare this type of nonresonant SH imaging to resonant SH imaging and two photon imaging using fluorophores.</p>","PeriodicalId":9053,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2023-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9611923","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Time-of-flight SIMS investigation of peptides containing cell penetrating sequences.","authors":"Alessandro Auditore, Nunzio Tuccitto, Giuseppe Grasso, Olivier Monasson, Elisa Peroni, Antonino Licciardello","doi":"10.1116/6.0002671","DOIUrl":"https://doi.org/10.1116/6.0002671","url":null,"abstract":"<p><p>Surface functionalization with biological molecules, such as peptides or proteins, is a very promising method for developing new biomaterials with many potential applications. However, due to their chemical complexity, the characterization of biological materials is often a very challenging task. In this context, time-of-flight secondary ion mass spectrometry is a very helpful characterization tool due to its ability to provide very detailed spatially resolved chemical information of the topmost layer. The peculiar emission/ion formation mechanisms involved in ToF-SIMS analysis often do not allow the detection of the molecular ion of proteins and peptides, providing a rich fragmentation pattern, which is difficult to be related to the surface composition using a univariate approach, due to the relevant number of peaks in the SIMS spectra of peptides and proteins and the slight differences in intensities between different samples. Therefore, we used multivariate analysis to extract the information contained in the ToF-SIMS spectra of four peptides with high amino acid sequence similarity along the peptide chain. The reference peptide (TAT1) is a 12-unit sequence of six amino acids (GRKKRRQRRRPS). The other three peptides have been obtained by inserting a bAla-H dipeptide (carnosine) in three different positions inside the TAT1 chain, namely, GRKKRRQRRRPS-bAla-H (TAT1-Car), bAla-HGRKKRRQRRRPS (Car-TAT1), and GRKKRRQ-bAla-H-RRRPS (T-Car-T). We show that these peptides can be distinguished by ToF-SIMS combined with multivariate data analysis.</p>","PeriodicalId":9053,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2023-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9981326","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BiointerphasesPub Date : 2023-05-01DOI: 10.1116/6.0002515
Qin Lu, Daniel P Regan, Daniel E Barlow, Kenan P Fears
{"title":"Antimicrobial efficacy of cyclic α- and β-peptides incorporated in polyurethane coatings.","authors":"Qin Lu, Daniel P Regan, Daniel E Barlow, Kenan P Fears","doi":"10.1116/6.0002515","DOIUrl":"10.1116/6.0002515","url":null,"abstract":"<p><p>Microbial growth on surfaces poses health concerns and can accelerate the biodegradation of engineered materials and coatings. Cyclic peptides are promising agents to combat biofouling because they are more resistant to enzymatic degradation than their linear counterparts. They can also be designed to interact with extracellular targets and intracellular targets and/or self-assemble into transmembrane pores. Here, we determine the antimicrobial efficacy of two pore-forming cyclic peptides, α-K3W3 and β-K3W3, against bacterial and fungal liquid cultures and their capacity to inhibit biofilm formation on coated surfaces. These peptides display identical sequences, but the additional methylene group in the peptide backbone of β-amino acids results in a larger diameter and an enhancement in the dipole moment. In liquid cultures, β-K3W3 exhibited lower minimum inhibitory concentration values and greater microbicidal power in reducing the number of colony forming units (CFUs) when exposed to a gram-positive bacterium, Staphylococcus aureus, and two fungal strains, Naganishia albida and Papiliotrema laurentii. To evaluate the efficacy against the formation of fungal biofilms on painted surfaces, cyclic peptides were incorporated into polyester-based thermoplastic polyurethane. The formation of N. albida and P. laurentii microcolonies (105 per inoculation) for cells extracted from coatings containing either peptide could not be detected after a 7-day exposure. Moreover, very few CFUs (∼5) formed after 35 days of repeated depositions of freshly cultured P. laurentii every 7 days. In contrast, the number of CFUs for cells extracted from the coating without cyclic peptides was >8 log CFU.</p>","PeriodicalId":9053,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2023-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9611922","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BiointerphasesPub Date : 2023-05-01DOI: 10.1116/6.0002720
Lara J Gamble, David Radford, David W Grainger, David G Castner
{"title":"Quantitative evaluation of perfluorinated alkanethiol molecular order on gold surfaces.","authors":"Lara J Gamble, David Radford, David W Grainger, David G Castner","doi":"10.1116/6.0002720","DOIUrl":"10.1116/6.0002720","url":null,"abstract":"<p><p>Self-assembled monolayers (SAMs) of perfluoroalkanethiols [CF3(CF2)xCH2CH2SH (x = 3, 5, 7, and 9)] on gold were characterized by x-ray photoelectron spectroscopy (XPS), near edge x-ray absorption fine structure (NEXAFS), and static time-of-flight secondary ion mass spectrometry (ToF-SIMS). Perfluoroalkanethiols of several chain lengths were synthesized using a known hydride reduction method for transforming commercially available perfluoroalkyliodides to corresponding perfluoroalkanethiols. This strategy provides improved product yields compared to other known routes based on hydrolysis from the common thioacetyl perfluoroalkyl intermediate. Angle-dependent XPS analysis revealed that CF3(CF2)xCH2CH2SH (x = 5, 7, and 9; F6, F8, and F10, respectively) SAMs on gold exhibited significant enrichment of the terminal CF3 group at the outer monolayer surface with the sulfur present as a metal-bound thiolate located at the monolayer-gold interface. XPS of the CF3(CF2)3CH2CH2SH (F4) monolayer revealed a thin film with a significant (>50%) amount of hydrocarbon contamination consistent with poorly organized monolayers, while the longest thiol (F10) showed XPS signals attributed to substantial ordering and anisotropy. ToF-SIMS spectra from all four SAMs contained molecular ions representative of the particular perfluorinated thiol used to prepare the monolayer. NEXAFS methods were used to determine degrees of ordering and average tilt for molecules comprising monolayers. The SAMs prepared from the longest (F10) thiols exhibited the highest degree of ordering with the molecular axis nearly perpendicular to the gold surface. The degree of ordering decreased significantly with decreasing length of the perfluorocarbon tail.</p>","PeriodicalId":9053,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":1.6,"publicationDate":"2023-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10264085/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9638866","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BiointerphasesPub Date : 2023-05-01DOI: 10.1116/6.0002489
Mohammadreza Aghaaminiha, Amir M Farnoud, Sumit Sharma
{"title":"Interdependence of cholesterol distribution and conformational order in lipid bilayers.","authors":"Mohammadreza Aghaaminiha, Amir M Farnoud, Sumit Sharma","doi":"10.1116/6.0002489","DOIUrl":"https://doi.org/10.1116/6.0002489","url":null,"abstract":"<p><p>We show, via molecular simulations, that not only does cholesterol induce a lipid order, but the lipid order also enhances cholesterol localization within the lipid leaflets. Therefore, there is a strong interdependence between these two phenomena. In the ordered phase, cholesterol molecules are predominantly present in the bilayer leaflets and orient themselves parallel to the bilayer normal. In the disordered phase, cholesterol molecules are mainly present near the center of the bilayer at the midplane region and are oriented orthogonal to the bilayer normal. At the melting temperature of the lipid bilayers, cholesterol concentration in the leaflets and the bilayer midplane is equal. This result suggests that the localization of cholesterol in the lipid bilayers is mainly dictated by the degree of ordering of the lipid bilayer. We validate our findings on 18 different lipid bilayer systems, obtained from three different phospholipid bilayers with varying concentrations of cholesterol. To cover a large temperature range in simulations, we employ the Dry Martini force field. We demonstrate that the Dry and the Wet Martini (with polarizable water) force fields produce comparable results.</p>","PeriodicalId":9053,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2023-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9521287","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BiointerphasesPub Date : 2023-05-01DOI: 10.1116/6.0002598
Jung-Eun Park, Yong-Seok Jang, Jae-Min Seo, Min-Ho Lee
{"title":"Facilitated osteogenesis of magnesium implant by coating of strontium incorporated calcium phosphate.","authors":"Jung-Eun Park, Yong-Seok Jang, Jae-Min Seo, Min-Ho Lee","doi":"10.1116/6.0002598","DOIUrl":"https://doi.org/10.1116/6.0002598","url":null,"abstract":"<p><p>This study investigated the corrosion resistance and biocompatibility of magnesium coated with strontium-doped calcium phosphate (Sr-CaP) for dental and orthopedic applications. Sr-CaP was coated on biodegradable magnesium using a chemical dipping method. Magnesium coated with Sr-CaP exhibited better corrosion resistance than pure magnesium. Sr-CaP-coated magnesium showed excellent cell proliferation and differentiation. Additionally, new bone formation was confirmed in vivo. Therefore, Sr-CaP-coated magnesium with reduced degradation and improved biocompatibility can be used for orthopedic and dental implant applications.</p>","PeriodicalId":9053,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2023-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9522596","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BiointerphasesPub Date : 2023-05-01DOI: 10.1116/6.0002604
Heba Khateb, Andrew L Hook, Stefanie Kern, Julie A Watts, Sonali Singh, Darryl Jackson, Luisa Marinez-Pomares, Paul Williams, Morgan R Alexander
{"title":"Identification of Pseudomonas aeruginosa exopolysaccharide Psl in biofilms using 3D OrbiSIMS.","authors":"Heba Khateb, Andrew L Hook, Stefanie Kern, Julie A Watts, Sonali Singh, Darryl Jackson, Luisa Marinez-Pomares, Paul Williams, Morgan R Alexander","doi":"10.1116/6.0002604","DOIUrl":"10.1116/6.0002604","url":null,"abstract":"<p><p>Secondary ion mass spectrometry (SIMS) offers advantages over both liquid extraction mass spectrometry and matrix assisted laser desorption mass spectrometry in that it provides the direct in situ analysis of molecules and has the potential to preserve the 3D location of an analyte in a sample. Polysaccharides are recognized as challenging analytes in the mass spectrometry of liquids and are also difficult to identify and assign using SIMS. Psl is an exopolysaccharide produced by Pseudomonas aeruginosa, which plays a key role in biofilm formation and maturation. In this Letter, we describe the use of the OrbiTrap analyzer with SIMS (3D OrbiSIMS) for the label-free mass spectrometry of Psl, taking advantage of its high mass resolving power for accurate secondary ion assignment. We study a P. aeruginosa biofilm and compare it with purified Psl to enable the assignment of secondary ions specific to the Psl structure. This resulted in the identification of 17 peaks that could confidently be ascribed to Psl fragments within the biofilm matrix. The complementary approach of the following neutral loss sequences is also shown to identify multiple oligosaccharide fragments without the requirement of a biological reference sample.</p>","PeriodicalId":9053,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":1.6,"publicationDate":"2023-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10234676/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10300156","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BiointerphasesPub Date : 2023-04-11DOI: 10.1116/6.0002502
Kangdi Sun, Tooba Shoaib, Mark W Rutland, Joseph Beller, Changwoo Do, Rosa M Espinosa-Marzal
{"title":"Insight into the assembly of lipid-hyaluronan complexes in osteoarthritic conditions.","authors":"Kangdi Sun, Tooba Shoaib, Mark W Rutland, Joseph Beller, Changwoo Do, Rosa M Espinosa-Marzal","doi":"10.1116/6.0002502","DOIUrl":"https://doi.org/10.1116/6.0002502","url":null,"abstract":"<p><p>Interactions between molecules in the synovial fluid and the cartilage surface may play a vital role in the formation of adsorbed films that contribute to the low friction of cartilage boundary lubrication. Osteoarthritis (OA) is the most common degenerative joint disease. Previous studies have shown that in OA-diseased joints, hyaluronan (HA) not only breaks down resulting in a much lower molecular weight (MW), but also its concentration is reduced ten times. Here, we have investigated the structural changes of lipid-HA complexes as a function of HA concentration and MW to simulate the physiologically relevant conditions that exist in healthy and diseased joints. Small angle neutron scattering and dynamic light scattering were used to determine the structure of HA-lipid vesicles in bulk solution, while a combination of atomic force microscopy and quartz crystal microbalance was applied to study their assembly on a gold surface. We infer a significant influence of both MW and HA concentrations on the structure of HA-lipid complexes in bulk and assembled on a gold surface. Our results suggest that low MW HA cannot form an amorphous layer on the gold surface, which is expected to negatively impact the mechanical integrity and longevity of the boundary layer and could contribute to the increased wear of the cartilage that has been reported in joints diseased with OA.</p>","PeriodicalId":9053,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":2.1,"publicationDate":"2023-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9356282","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}