Amyloidosis are metabolic conformational diseases caused by misfolding and aggregation of soluble proteins in insoluble fibrils which deposit squeezing out the functioning cells or block cell-to-cell connectivity. Amylin or Islet Amyloid Polypeptide (IAPP) is a 37 residue peptide hormone secreted by pancreatic β-cells together with insulin. Amylin forms deposits in pancreas and is a non-insulin-dependent type II diabetes disease agent. Six stranded single ß-sheets of amylin 10-29 residues QRLANFLVHSSNNFGAILSS (Amylin 10-29), was investigated by molecular dynamics (MD) simulations in a periodic box using Amber 9.0, f99 force field and isothermal-isobaric ensemble, NTP protocol (constant temperature, pressure and the number of particles). The total MD run was 193 ns for Amylin 10-29. MD simulations show that a) Amylin 10-29 ß-sheet is bound together mainly by backbone hydrogen bonding, b) The ß-sheet is stabilized by side chain hydrogen bonding between asparagine residues and between residues Ser20 and Asp22 c). The ß-strands of Amylin 10-29 are glued together by leucine, isoleucine, valine residues and by phenylalanine residues, which together with asparagine residues form a sub-stack kept together by mild polar interactions, d) The C terminal part of the Amylin 10-29 ß-sheet has the hydrophobic anchor of isoleucine and leucine residues Ile26-Leu27 which could be used to bind nearby ß-sheets in the ß-sheet protofibril. This binding should stabilize the ß-structure of a separate ß-sheet. e). In the Amylin 10-29 region Ser19-Ser20-Asn21-Asn22 the ß-sheet has the W-shaped bend with the deeper vertex on Ser20 and smaller vertex on Asn22, suggesting that also the bent ß-sheet could be possible.