Investigating Structure and Dynamics of Atg8 Family Proteins.

Atg8 family members were the first autophagy-related proteins to be investigated in structural detail and continue to be among the best-understood molecules of the pathway. In this review, we will first provide a concise outline of the major methods that are being applied for structural characterization of these proteins and the complexes they are involved in. This includes a discussion of the strengths and limitations associated with each method, along with guidelines for successful adoption to a specific problem. Subsequently, we will present examples illustrating the application of these techniques, with a particular focus on the complementarity of information they provide.

Amyloid aggregation inhibitory mechanism of arginine-rich D-peptides.

It is widely believed that Alzheimer's disease pathogenesis is driven by the production and deposition of the amyloid-ß peptide (Aß) in the brain. In this study, we employ a combination of in silico and in vitro approaches to investigate the inhibitory properties of selected arginine-rich D-enantiomeric peptides (D-peptides) against amyloid aggregation. The D-peptides include D3, a 12-residue peptide with anti-amyloid potencies demonstrated in vitro and in vivo, RD2, a scrambled sequence of D3, as well as truncated RD2 variants. Using a global optimization method together with binding free energy calculations followed by molecular dynamics simulations, we perform a detailed analysis of D-peptide binding to Aß monomer and a fibrillar Aß structure. Results obtained from both molecular simulations and surface plasmon resonance experiments reveal a strong binding of D3 and RD2 to Aß, leading to a significant reduction in the amount of ß structures in both monomer and fibril, which was also demonstrated in Thioflavin T assays. The binding of the D-peptides to Aß is driven by electrostatic interactions, mostly involving the D-arginine residues and Glu11, Glu22 and Asp23 of Aß. Furthermore, we show that the anti-amyloid activities of the D-peptides depend on the length and sequence of the Dpeptide, its ability to form multiple weak hydrophobic interactions with Aß, as well as the Aß oligomer size.

The effects of spastic cerebral palsy on occlusion.

This research paper compares dental casts and lateral cephalometric radiographs of thirty children with spastic cerebral palsy with those of a control group to determine what effect spasticity and cerebral palsy have on dental occlusion and skeletal formation. Muscle spasticity can retard bone growth. Variations in the normal tonus of head and neck muscles can cause malocclusion and arch deformity.

Letterer-Siwe disease: report of case.

Initial oral symptoms of Letterer-Siwe disease reveal the importance of a dentist in establishing this diagnosis. This case is important in that the patient was five months old, at which time an early diagnosis was made and treatment had begun. Because most cases occur in young children, a high level of suspicion is necessary, because the oral manifestations and radiographic findings in children may often resemble the periapical, periodontal or cystic involvements frequently seen first by the dentist. The oral lesions were necrotic, hemorrhagic, and degenerative gingival tissues in the maxillary molar area. Loss of alveolar bone was evident. There was precocious eruption of seven primary teeth, which were slightly mobile. Dentally, prophylaxis and fluoride applications were supportive measures.