Removal of Photoresist Film Residues from Wafer Surfaces

Peters, D. A.; Deckert, C. A.

doi:10.1149/1.2129162

Cited by 20 publications

(11 citation statements)

References 1 publication

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“…After ten rinsings in distilled water, the inorganic contaminations on substrates were removed by washing for 5 min at 80°C in 6:1:1 parts of distilled water, hydrogen peroxide (30% v/v), and hydrochloric acid (37% v/v). This yielded a thin hydrated surface layer of SiO 2 33, 34 (water/surface static contact angle, θ w , <10°, when measured with a Ramé‐Hart NRL Model 100 goniometer, USA).…”

Section: Methodsmentioning

confidence: 99%

Interactions between surface‐bound actin and complement, platelets, and neutrophils

Wetterö

Askendal

Tengvall

et al. 2003

J Biomedical Materials Res

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Actin exists as globular (G) monomers or polymeric filaments (F) in the cytoplasm of eukaryotic cells and mediates cell morphological changes and motility. Large amounts of this protein may be released out to the extracellular compartment during tissue injury, but little is known about its role in biomaterialrelated inflammation. We immobilized actin to methylated glass, methylated-and aminated silicon and gold model surfaces and studied subsequent blood serum deposition and complement activation, generation of reactive oxygen species (ROS), and adhesion and aggregation of neutrophils and platelets. Nullellipsometry shows that approximately one monolayer of G-actin can be immobilized onto the model surfaces and actin in buffer polymerizes on top of this by the addition of K + and Mg 2+ ions to form a thicker layer of firmly bound F-actin. F-actin bound after serum incubation low amounts of anti-complement factor 1q (anti-C1q). The analysis of cell responses upon contact with actin-coated surfaces by luminol-amplified chemiluminescence, lumi-aggregometry and fluorescence microscopy show that surface-triggered aggregation, spreading, and generation of ROS were down-regulated and comparable to the response by adsorbed albumin. However, F-actin on gold surfaces recruited platelets in a C1q-dependent manner. We conclude that adsorbed actin in vitro is a weak complement, platelet and neutrophil activator, although Factin associates with both C1q and platelets.

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Section: Methodsmentioning

confidence: 99%

Interactions between surface‐bound actin and complement, platelets, and neutrophils

Wetterö

Askendal

Tengvall

et al. 2003

J Biomedical Materials Res

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“…Silicon wafers (Okmetic LMTD, Esbo, Finland) cleaved into 5 × 10‐mm pieces in the (100) crystal direction, 76 × 26 mm Microscope Slides (Menzel‐Gläser, Braunschweig, Germany, 72.2% SiO 2 ) or 40 × 8 mm glass test tubes (Assistent KHG, Sondheim‐Rhön, Germany, approximately 75% SiO 2 ) were cleaned for 5 min at 80°C in distilled (Milli‐Q) water, hydrogen peroxide (30% v/v) and NH 4 OH (25% v/v), 5 : 1 : 1 parts respectively 28, 29. The surfaces were then rinsed ten times in distilled water and incubated for another 5 min at 80°C in distilled water, hydrogen peroxide, and hydrochloric acid (37% v/v), 6 : 1 : 1 parts, respectively.…”

Section: Methodsmentioning

confidence: 99%

C1q-independent activation of neutrophils by immunoglobulin M-coated surfaces

Wetterö

Bengtsson

Tengvall

2001

J. Biomed. Mater. Res.

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Neutrophil granulocytes are known to rapidly adhere and undergo frustrated phagocytosis upon contact with immunoglobulin and/or complement protein opsonized artificial surfaces. In this study, we examined the relation between serum protein deposition and human neutrophil activation on hydrophobic glass and silicon model surfaces that were coated with immunoglobulin G or M (IgG/IgM), both initiators of the classical complement pathway. Protein adsorption from normal human serum (NHS) was quantified with null-ellipsometry combined with antibody techniques. The neutrophil oxygen radical production was registered by luminol-amplified chemiluminescence (CL) and the morphology, as well as changes in the content of filamentous actin (F-actin), was documented by fluorescence microscopy. Complement factor 3 (C3) bound to both IgG-and IgM-coated surfaces, but surprisingly C1q was found only on IgG-coated surfaces. Both immunoglobulins triggered complement dependent neutrophil activation. However, CL and F-actin accumulation were found sensitive to the presence of C1q in serum only at the IgG-coated surface. We suggest that spontaneously adsorbed IgM activates the complement system and interacts with neutrophils by C1q-independent mechanisms.

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“…Thereafter, the wafers were "boiled" for 5 minutes at 80°C in six parts of distilled water, one part of hydrogen peroxide (30% v/v) and one part of hydrochloric acid (37% v/v), resulting in a thin hydrated surface layer of SiO 2 [23,24]. The water/surface static contact angle (θ w ) was less than 10° (Ramé-Hart NRL Model 100 goniometer, USA).…”

Section: Hydrophobic Surfacesmentioning

confidence: 99%

On the binding of complement to solid artificial surfaces in vitro

et al. 2002

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Since the realization of a complement activation capacity by artificial surfaces upon contact with blood, a common belief has evolved that charged nucleophilic surface groups such as amine (-NH 2 ) and hydroxyl (-OH) react with and eventually bind to the internal thioester in complement factor 3 (C3). A covalent ester or amide linkage is thereby supposed to form between C3b and the surface itself. In this report,we present complement surface binding data by null-ellipsometry for two nucleophilic surfaces (-NH 2 and -OH), for surfaces with immunoglobulin G (IgG) covalently bound, and for IgG spontaneously pre-adsorbed to hydrophobic silicon. The results reveal that the plasma proteins that were deposited during complement activation became eluted by sodium dodecyl sulfate (SDS). Hence the direct covalent binding between C3 and solid nucleophilic surfaces seems to be only of moderate importance, at least during shorter serum incubations. This strongly suggests that the prevalent covalent linkage model between solid artificial surfaces and C3b is not accurate.Instead we suggest a more pronounced role for C3 associations to other adsorbed proteins and/or electrostatic and hydrophobic protein-surface interactions.

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Removal of Photoresist Film Residues from Wafer Surfaces

Abstract: not Available.

Cited by 20 publications

References 1 publication

Interactions between surface‐bound actin and complement, platelets, and neutrophils

Interactions between surface‐bound actin and complement, platelets, and neutrophils

C1q-independent activation of neutrophils by immunoglobulin M-coated surfaces

On the binding of complement to solid artificial surfaces in vitro

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