Purpose Current recommendations for refeeding in anorexia nervosa (AN) are conservative, beginning around 1,200 calories to avoid refeeding syndrome. We previously showed poor weight gain and long hospital stay using this approach and hypothesized that a higher calorie approach would improve outcomes. Methods Adolescents hospitalized for malnutrition due to AN were included in this quasi-experimental study comparing lower and higher calories during refeeding. Participants enrolled between 2002 and 2012; higher calories were prescribed starting around 2008. Daily prospective measures included weight, heart rate, temperature, hydration markers and serum phosphorus. Participants received formula only to replace refused food. Percent Median Body Mass Index (% MBMI) was calculated using 50th percentile body mass index for age and sex. Unpaired t-tests compared two groups split at 1,200 calories. Results Fifty-six adolescents with mean (±SEM) age 16.2 (±.3) years and admit %MBMI 79.2% (±1.5%) were hospitalized for 14.9 (±.9) days. The only significant difference between groups (N = 28 each) at baseline was starting calories (1,764 [±60] vs. 1,093 [±28], p < .001). Participants on higher calories had faster weight gain (.46 [±.04] vs. .26 [±.03] %MBMI/day, p < .001), greater daily calorie advances (122 [±8] vs. 98 [±6], p = .024), shorter hospital stay (11.9 [±1.0] vs. 17.6 [±1.2] days, p < .001), and a greater tendency to receive phosphate supplementation (12 vs. 8 participants, p = .273). Conclusions Higher calorie diets produced faster weight gain in hospitalized adolescents with AN as compared with the currently recommended lower calorie diets. No cases of the refeeding syndrome were seen using phosphate supplementation. These findings lend further support to the move toward more aggressive refeeding in AN.

Performing nutrition assessment remotely via telehealth is a topic of significant interest given the global pandemic in 2020 that has necessitated physical distancing and virtual communications. This review presents an evidence‐based approach to conducting nutrition assessments remotely. The authors present suggestions for adaptations that can be used to perform a remote nutrition‐focused physical exam. Direct‐to‐consumer technologies that can be used in remote nutrition assessment are discussed and compared. Practice tips for conducting a telehealth visit are also presented. The aim of this publication is to provide interdisciplinary clinicians a set of guidelines and best practices for performing nutrition assessments in the era of telehealth.

The N-terminal 146 residues of apolipoprotein (apo) A-V adopt a helix bundle conformation in the absence of lipid. Because similarly sized truncation mutants in human subjects correlate with severe hypertriglyceridemia, the lipid binding properties of apoA-V(1-146) were studied. Upon incubation with phospholipid in vitro, apoA-V(1-146) forms reconstituted high density lipoproteins 15-17 nm in diameter. Far UV circular dichroism spectroscopy analyses of lipid-bound apoA-V(1-146) yielded an ␣-helix secondary structure content of 60%. Fourier transformed infrared spectroscopy analysis revealed that apoA-V(1-146) ␣-helix segments align perpendicular with respect to particle phospholipid fatty acyl chains. Fluorescence spectroscopy of single Trp variant apoA-V(1-146) indicates that lipid interaction is accompanied by a conformational change. The data are consistent with a model wherein apoA-V(1-146) ␣-helices circumscribe the perimeter of a disk-shaped bilayer. The ability of apoA-V(1-146) to solubilize dimyristoylphosphatidylcholine vesicles at a rate faster than full-length apoA-V suggests that N-and C-terminal interactions in the full-length protein modulate its lipid binding properties. Preferential association of apoA-V(1-146) with murine plasma HDL, but not with VLDL, suggests that particle size is a determinant of its lipoprotein binding specificity. It may be concluded that defective lipoprotein binding of truncated apoA-V contributes to the hypertriglyceridemia phenotype associated with truncation mutations in human subjects.The helix bundle motif is a common molecular architecture in proteins (1). Exchangeable apolipoproteins (apo) 4 are known to adopt this conformation, which supports their dual existence in alternate lipid-free and lipid-bound states. Classic examples of the helix bundle structure include the N-terminal (NT) domains of apoE (2) and apoA-I (3) as well as apolipophorin III (4). In the case of apoE and apoA-I, the helix bundle motifs are present within the context of a larger protein structure. In each of these examples the bundle exists as an up-and-down series of amphipathic ␣-helices wherein the hydrophobic face of each helical segment orients toward the interior of the bundle. At the same time, the polar face of the amphipathic helices is directed toward the exterior of the bundle. In this way the globular structure is stabilized by hydrophobic helix-helix interactions and is conferred with water solubility through projection of polar and charged amino acid side chains toward the aqueous milieu. Upon interaction with lipid surfaces, the helix bundle is postulated to unfurl, adopting an extended open conformation that promotes interaction between the hydrophobic faces of amphipathic helices and the lipid surface. Essentially, lipid binding of helix bundle apolipoproteins substitutes helix-helix contacts in the bundle for helix-lipid contacts that stabilize the lipid-bound state.In 2001 a new apolipoprotein, termed apoA-V, was reported that profoundly affects plasma TG levels (5, 6). Str...

Purpose of review Computing advances over the decades have catalyzed the pervasive integration of digital technology in the medical industry, now followed by similar applications for clinical nutrition. This review discusses the implementation of such technologies for nutrition, ranging from the use of mobile apps and wearable technologies to the development of decision support tools for parenteral nutrition and use of telehealth for remote assessment of nutrition. Recent findings Mobile applications and wearable technologies have provided opportunities for real-time collection of granular nutrition-related data. Machine learning has allowed for more complex analyses of the increasing volume of data collected. The combination of these tools has also translated into practical clinical applications, such as decision support tools, risk prediction, and diet optimization. Summary The state of digital technology for clinical nutrition is still young, although there is much promise for growth and disruption in the future.

Recently released recommendations for detection and documentation of malnutrition in adults in clinical practice define 3 types of malnutrition: starvation related, acute disease or injury related, and chronic disease related. The first 2 are more easily recognized, but the third may be more often unnoticed, particularly in obese patients. Critical care patients tend to be at high risk for malnutrition and thus require a thorough nutritional assessment. Compared with patients of earlier times, intensive care unit patients today tend to be older, have more complex medical and comorbid conditions, and often are obese. Missed or delayed detection of malnutrition in these patients may contribute to increases in hospital morbidity and longer hospital stays. Critical care nurses are in a prime position to screen patients at risk for malnutrition and to work with members of the interprofessional team in implementing nutritional intervention plans.

Current healthcare is weight-centric, equating weight and health. This approach to healthcare has negative consequences on patient well-being. The aim of this article is to make a case for a paradigm shift in how clinicians view and address body weight. In this review, we (1) address common flawed assumptions in the weight-centric approach to healthcare, (2) review the weight science literature and provide evidence for the negative consequences of promoting dieting and weight loss, and (3) provide practice recommendations for weight-inclusive care.

Background: Adequate nutrition (receiving ࣙ80% of estimated energy requirements [EER]) is important in preventing and treating malnutrition and improving clinical outcomes. In conventional rate-based tube feeding (RBTF), patients are prescribed a constant infusion rate. Per volume-based tube feeding (VBTF), the hourly infusion rate can be increased (max 150 mL/h) to make up for feeding deficits, ensuring patients receive the targeted 24-hour volume. This study compared clinical outcomes between patients on VBTF vs RBTF. Methods: Data were collected from medical charts of patients within a 5-month period. Inclusion criteria included patients ࣙ18 years of age who were admitted to an intensive care unit and receiving enteral nutrition for at least 24 hours.

Apolipoprotein (apo) A-V is a 343 residue, multi-domain protein that plays an important role in regulation of plasma triglyceride homeostasis. Primary sequence analysis revealed a unique tetraproline sequence (Pro293 -Pro296) near the carboxyl terminus of the protein. A peptide corresponding to the 48 residue segment beyond the tetra-proline motif was generated from a recombinant apoA-V precursor wherein Pro295 was replaced by Met. Cyanogen bromide cleavage of the precursor protein, followed by negative affinity chromatography, yielded a purified peptide. Nondenaturing polyacrylamide gel electrophoresis verified that apoA-V(296-343) solubilizes phospholipid vesicles, forming a relatively heterogeneous population of reconstituted high density lipoprotein with Stoke's diameters > 17 nm. At the same time, apoA-V(296-343) failed to bind a spherical lipoprotein substrate in vitro. Far UV circular dichroism spectroscopy revealed the peptide is unstructured in buffer yet adopts significant α-helical secondary structure in the presence of the lipid mimetic solvent, trifluoroethanol (TFE; 50% v/v). Heteronuclear multidemensional NMR spectroscopy experiments were conducted with uniformly 15 N and 15 N/ 13 C labeled peptide in 50 % TFE. Peptide backbone assignment and secondary structure prediction using TALOS+ reveals the peptide adopts α-helix secondary structure from residues 309 -334. In TFE, apoA-V(296-343) adopts an extended amphipathic α-helix, consistent with a role in lipoprotein binding as a component of full-length apoA-V.Apolipoprotein (apo) A-V was discovered in 2001 in a comparative genomics study (1) and as an mRNA up-regulated during rat liver regeneration (2). Subsequent research has shown that apoA-V serves as a potent modulator of plasma triacylglycerol (TG) homeostasis. Mature apoA-V is a non-glycosylated protein comprised of 343 amino acids. An interesting feature of apoA-V is the presence of four consecutive Pro near the carboxyl (C)-terminus (Pro293 -Pro296). Indeed, this sequence element in apoA-V is conserved across species including human, rat, mouse, olive baboon, cow, wild boar and dog but not frog or chicken. Whereas the 47 residue segment C-terminal to the tetra-proline sequence in human apoA-V was postulated to comprise an independent structural domain, guanidine HCl denaturation studies showed this segment comprises part of a larger C-terminal domain (3). A recombinant C-terminal truncated apoA-V, missing the region beyond residue 292, displayed defective lipid binding activity compared to full-length apoA-V. Furthermore, in the absence of a C-terminal domain, the Nterminal domain of apoA-V (residues 1-146) loses its capacity to bind larger lipoprotein substrates, such as very low density lipoprotein (4). When taken together with observations that naturally occurring C-terminal truncated apoA-V mutants in humans are associated with severe hypertriglyceridemia (HTG) (5,6), it is conceivable that residues 296-343 of apoA-V are required for proper functioning of this protein.In the pres...