New mobile methods for dietary assessment: review of image-assisted and image-based dietary assessment methods.

For nutrition practitioners and researchers, assessing dietary intake of children and adults with a high level of accuracy continues to be a challenge. Developments in mobile technologies have created a role for images in the assessment of dietary intake. The objective of this review was to examine peer-reviewed published papers covering development, evaluation and/or validation of image-assisted or image-based dietary assessment methods from December 2013 to January 2016. Images taken with handheld devices or wearable cameras have been used to assist traditional dietary assessment methods for portion size estimations made by dietitians (image-assisted methods). Image-assisted approaches can supplement either dietary records or 24-h dietary recalls. In recent years, image-based approaches integrating application technology for mobile devices have been developed (image-based methods). Image-based approaches aim at capturing all eating occasions by images as the primary record of dietary intake, and therefore follow the methodology of food records. The present paper reviews several image-assisted and image-based methods, their benefits and challenges; followed by details on an image-based mobile food record. Mobile technology offers a wide range of feasible options for dietary assessment, which are easier to incorporate into daily routines. The presented studies illustrate that image-assisted methods can improve the accuracy of conventional dietary assessment methods by adding eating occasion detail via pictures captured by an individual (dynamic images). All of the studies reduced underreporting with the help of images compared with results with traditional assessment methods. Studies with larger sample sizes are needed to better delineate attributes with regards to age of user, degree of error and cost.

Structure-function relationships of des-(B26-B30)-insulin.

In order to study the role of the amino acid in position B25 and its environment in shortened insulins, a series of analogues was prepared with the following modifications: 1, Stepwise shortening of the B-chain including replacements of TyrB26 and ThrB27 by glycine; 2, substitutions at the carboxamide nitrogen of des-(B26-B30)-insulin-B25-amide by apolar, polar or charged residues of various chain lengths; 3, replacement of PheB25 by asparagine-amide, phenylalaninol or a series of alkyl and aralkyl residues. Trypsin-catalyzed semisyntheses were performed with Boc-protected or unprotected des-octapeptide-(B23-B30)-insulin and synthetic peptides. Relative receptor binding and in vitro bioactivity of [AsnB25]-des-(B26-B30)-insulin-B25-amide was 227 and 292% (on insulin), other activities ranged between 1 and ca. 200%. We make the following conclusions. An L-amino acid is essential in position B25. The B25-carbonyl and NH groups favour high binding and "superpotency", but are not indispensible for receptor contacts. For high affinity receptor interaction, the planarity at the C gamma-atom and the distance of B25-side-chain branching in position B25 are important, but an aromatic ring is not necessary.

Shortened insulin with enhanced in vitro potency.

After it has been shown that removal of residues B26-B30 leaves insulin with full biological activity, provided the new C-terminus is amidated (Fischer et al. (1985) Biol. Chem. Hoppe-Seyler 366, 521-525), it is demonstrated here that it does not even preclude enhancement of potency. 7 analogues of des-(B26-B30)-insulin-B25-amide were prepared by trypsin-mediated semisynthesis, the replacements being D-PheB24; HisB25, D-PheB25, TrpB25, TyrB25; D-PheB24,B25 and D-PheB24, TyrB25. Mere conversion of the configuration of B25-phenylalanine reduces in vitro potency to 0.5%. If B25-phenylalanine is, however, substituted by histidine or tyrosine activity is increased to 310 or 230, respectively. According to the features common to these two side chains, the favourable effect should be due to their ring structure with balanced aromatic and polar or H-bonding properties, respectively. The results indicate that in the complete insulin molecule the C-terminal pentapeptide modulates the subtle role that residues B24 and/or B25 play in receptor binding and activity; its presence may have a positive or negative effect. The drastic differences in activity between the shortened analogues are in no ways reflected in the CD spectra which are very similar, though clearly different from that of native insulin.