Mannan-binding lectin: structure, oligomerization, and flexibility studied by atomic force microscopy.

Mannan-binding lectin (MBL) is the archetypical pathogen recognition molecule of the innate immune defense. Upon binding to microorganisms, reactions leading to the destruction of the offender ensue. MBL is an oligomer of structural subunits each composed of three identical polypeptides.

A common polymorphism in the SFTPD gene influences assembly, function, and concentration of surfactant protein D.

Surfactant protein D (SP-D) plays important roles in the host defense against infectious microorganisms and in regulating the innate immune response to a variety of pathogen-associated molecular pattern. SP-D is mainly expressed by type II cells of the lung, but SP-D is generally found on epithelial surfaces and in serum. Genotyping for three single-nucleotide variations altering amino acids in the mature protein in codon 11 (Met(11)Thr), 160 (Ala(160)Thr), and 270 (Ser(270)Thr) of the SP-D gene was performed and related to the SP-D levels in serum.

Adsorption kinetics and mechanical properties of thiol-modified DNA-oligos on gold investigated by microcantilever sensors.

Immobilised DNA-oligo layers are scientifically and technologically appealing for a wide range of sensor applications such as DNA chips. Using microcantilever-based sensors with integrated readout, we demonstrate in situ quantitative studies of surface-stress formation during self-assembly of a 25-mer thiol-modified DNA-oligo layer. The self-assembly induces a surface-stress change, which closely follows Langmuir adsorption model.

Environmental sensors based on micromachined cantilevers with integrated read-out.

An AFM probe with integrated piezoresistive read-out has been developed and applied as a cantilever-based environmental sensor. The probe has a built-in reference cantilever, which makes it possible to subtract background drift directly in the measurement. Moreover, the integrated read-out facilitates measurements in liquid.