Compensating for memory losses throughout aging: validation and normalization of the memory compensation questionnaire (MCQ) for non-clinical French populations.

AIM: The MCQ is a seven-factor scale that measures individual differences in the tendency to select particular strategies and to overcome perceived or real memory losses. Our aim was to establish a French version of the MCQ and to evaluate its psychometric properties in a lifespan perspective. We first tested the underlying factor structure of the MCQ in a large sample of 749 adults from aged from 18 to 92 years. RESULTS: The results showed that the factor structure of the French version corresponded well with the one obtained in English-, Dutch- and Spanish-speaking samples, supporting the cross-national robustness of the MCQ. We confirmed a seven-factor order model that supports the construct validity of the questionnaire. The reliabilities of the scales were good (α>.70) to acceptable (α=.66 and .62). Criterion validity was verified by means of significant correlations between health composites and MCQ subscales. Gender and Age affected most of the MCQ subscales but not the Level of Education (LE). CONCLUSION: The MCQ revealed to be a heuristic tool for assessing daily compensatory behaviors that are developed in order to achieve successful aging. Thus, regression-based normative data and a user-friendly computer program were provided to facilitate scoring and norming by clinicians and researchers who need to assess daily compensatory behaviors.

Age differences in outdated information processing during news reports reading.

In two experiments, the authors explored whether there are any age differences associated with the ability to process outdated information during news reports comprehension. Younger and older participants (mean age: 70 years old) read passages in which a cause was first said to be responsible for the occurrence of a news event. New elements emerged from the investigation in progress and revealed that the original cause was incorrect. Inference response times indicated that older adults more than younger ones took advantage of an alternative cause mentioned in the text to put the outdated information in the background, whereas younger readers probably kept both causes activated. The research tested the concepts involved with age differences in updating situation model.

Directed assembly of functional light harvesting antenna complexes onto chemically patterned surfaces.

We report the directed assembly of the photosynthetic membrane proteins LH1 and LH2 isolated from the purple bacterium Rhodobacter sphaeroides onto chemically patterned substrates. Nanoimprint lithography was used to pattern discrete regions of amino- and fluoro-terminated or poly(ethylene glycol) self-assembled monolayers onto a glass substrate. Densely packed layers of assembled protein complexes were observed with atomic force microscopy. The protein complexes attached selectively to the amino-terminated regions by electrostatic interactions. Spectral images generated with a hybrid scanning probe and fluorescence microscope confirmed that the patterned proteins retained their native optical signatures.

Creating nanopatterns of His-tagged proteins on surfaces by nanoimprint lithography using specific NiNTA-histidine interactions.

Directed assembly of the DsRed FT protein is demonstrated on self-assembled monolayers (SAMs) on silicon substrates patterned by nanoimprint lithography. Initially, the DsRed protein is attached using electrostatic interactions on both topographical (polymer) templates with an amino functionalization and on chemically patterned (flat) substrates. In a second experiment, a patterned NiNTA SAM is used in order to attach the DsRed FT protein via supramolecular interactions, taking advantage of the histidine functionalization of the DsRed FT protein. The NTA SAM is formed on silicon oxide using a multistep covalent process. Patterning of the NTA SAM is performed using nanoimprint lithography. The DsRed FT protein is attached on the patterned NTA layer after treating this with a Ni(II) solution. Moreover, the histidine-NiNTA binding may be reversed by removing the Ni using EDTA or by competition using imidazole. The regeneration and reuse of the substrate by subsequently attaching and removing two different histidine-functionalized proteins from the patterned NTA is shown by fluorescence microscopy.